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NeuraminidaseZanamivirSialic AcidsOseltamivirInfluenza A virusPyransNeuraminic AcidsOrthomyxoviridaeN-Acetylneuraminic AcidHemagglutinin Glycoproteins, Influenza VirusInfluenza, HumanHemagglutination, ViralGuanidinesAntiviral AgentsInfluenza A Virus, H1N1 SubtypeHemagglutinins, ViralOrthomyxoviridae InfectionsInfluenza B virusInfluenza A Virus, H3N2 SubtypeInfluenza A Virus, H5N1 SubtypeInfluenza in BirdsDrug Resistance, ViralGalactose OxidaseFerretsHemagglutination Inhibition TestsHemagglutininsHN ProteinReassortant VirusesLectinsAcetamidesInfluenza A Virus, H2N2 SubtypeInfluenza A Virus, H7N9 SubtypeInfluenza A Virus, H9N2 SubtypeDogsNewcastle disease virusInfluenza VaccinesClostridium perfringensViral ProteinsCell LineGlycoproteinsWheat Germ AgglutininsParainfluenza Virus 3, HumanMadin Darby Canine Kidney CellsCarbohydratesHemadsorptionPeanut AgglutininDucksBirdsCathepsin AReceptors, VirusGangliosidesViral Plaque AssayCyclopentanesGlycosylationHemagglutination TestsParamyxoviridaeMolecular Sequence DataHymecromoneErythrocytesPeriodic AcidGlycoside HydrolasesEnzyme InhibitorsMucolipidosesMolecular WeightHemagglutinationAntibodies, ViralArthrobacterPandemicsAmantadineChick EmbryoVirus ReplicationSialoglycoproteinsPronaseElectrophoresis, Polyacrylamide GelTrypsinPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidaseActinomycetaceaeCell MembraneChickensParainfluenza Virus 1, HumanIsoelectric FocusingRespirovirusAmino Acid SequenceMutationEpitopesMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseOxo-Acid-Lyases
Neuraminidase: An enzyme that catalyzes the hydrolysis of alpha-2,3, alpha-2,6-, and alpha-2,8-glycosidic linkages (at a decreasing rate, respectively) of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid, and synthetic substrate. (From Enzyme Nomenclature, 1992)Zanamivir: A guanido-neuraminic acid that is used to inhibit NEURAMINIDASE.Sialic Acids: A group of naturally occurring N-and O-acyl derivatives of the deoxyamino sugar neuraminic acid. They are ubiquitously distributed in many tissues.Oseltamivir: An acetamido cyclohexene that is a structural homolog of SIALIC ACID and inhibits NEURAMINIDASE.Influenza A virus: The type species of the genus INFLUENZAVIRUS A that causes influenza and other diseases in humans and animals. Antigenic variation occurs frequently between strains, allowing classification into subtypes and variants. Transmission is usually by aerosol (human and most non-aquatic hosts) or waterborne (ducks). Infected birds shed the virus in their saliva, nasal secretions, and feces.PyransNeuraminic AcidsOrthomyxoviridae: A family of RNA viruses causing INFLUENZA and other diseases. There are five recognized genera: INFLUENZAVIRUS A; INFLUENZAVIRUS B; INFLUENZAVIRUS C; ISAVIRUS; and THOGOTOVIRUS.N-Acetylneuraminic Acid: An N-acyl derivative of neuraminic acid. N-acetylneuraminic acid occurs in many polysaccharides, glycoproteins, and glycolipids in animals and bacteria. (From Dorland, 28th ed, p1518)Hemagglutinin Glycoproteins, Influenza Virus: Membrane glycoproteins from influenza viruses which are involved in hemagglutination, virus attachment, and envelope fusion. Fourteen distinct subtypes of HA glycoproteins and nine of NA glycoproteins have been identified from INFLUENZA A VIRUS; no subtypes have been identified for Influenza B or Influenza C viruses.Influenza, Human: An acute viral infection in humans involving the respiratory tract. It is marked by inflammation of the NASAL MUCOSA; the PHARYNX; and conjunctiva, and by headache and severe, often generalized, myalgia.Hemagglutination, Viral: Agglutination of ERYTHROCYTES by a virus.Guanidines: A family of iminourea derivatives. The parent compound has been isolated from mushrooms, corn germ, rice hulls, mussels, earthworms, and turnip juice. Derivatives may have antiviral and antifungal properties.Antiviral Agents: Agents used in the prophylaxis or therapy of VIRUS DISEASES. Some of the ways they may act include preventing viral replication by inhibiting viral DNA polymerase; binding to specific cell-surface receptors and inhibiting viral penetration or uncoating; inhibiting viral protein synthesis; or blocking late stages of virus assembly.Influenza A Virus, H1N1 Subtype: A subtype of INFLUENZA A VIRUS with the surface proteins hemagglutinin 1 and neuraminidase 1. The H1N1 subtype was responsible for the Spanish flu pandemic of 1918.Hemagglutinins, Viral: Specific hemagglutinin subtypes encoded by VIRUSES.Orthomyxoviridae Infections: Virus diseases caused by the ORTHOMYXOVIRIDAE.Influenza B virus: Species of the genus INFLUENZAVIRUS B that cause HUMAN INFLUENZA and other diseases primarily in humans. Antigenic variation is less extensive than in type A viruses (INFLUENZA A VIRUS) and consequently there is no basis for distinct subtypes or variants. Epidemics are less likely than with INFLUENZA A VIRUS and there have been no pandemics. Previously only found in humans, Influenza B virus has been isolated from seals which may constitute the animal reservoir from which humans are exposed.Influenza A Virus, H3N2 Subtype: A subtype of INFLUENZA A VIRUS comprised of the surface proteins hemagglutinin 3 and neuraminidase 2. The H3N2 subtype was responsible for the Hong Kong flu pandemic of 1968.Influenza A Virus, H5N1 Subtype: A subtype of INFLUENZA A VIRUS comprised of the surface proteins hemagglutinin 5 and neuraminidase 1. The H5N1 subtype, frequently referred to as the bird flu virus, is endemic in wild birds and very contagious among both domestic (POULTRY) and wild birds. It does not usually infect humans, but some cases have been reported.Influenza in Birds: Infection of domestic and wild fowl and other BIRDS with INFLUENZA A VIRUS. Avian influenza usually does not sicken birds, but can be highly pathogenic and fatal in domestic POULTRY.Drug Resistance, Viral: The ability of viruses to resist or to become tolerant to chemotherapeutic agents or antiviral agents. This resistance is acquired through gene mutation.Galactose Oxidase: An enzyme that oxidizes galactose in the presence of molecular oxygen to D-galacto-hexodialdose. It is a copper protein. EC 1.1.3.9.Ferrets: Semidomesticated variety of European polecat much used for hunting RODENTS and/or RABBITS and as a laboratory animal. It is in the subfamily Mustelinae, family MUSTELIDAE.Hemagglutination Inhibition Tests: Serologic tests in which a known quantity of antigen is added to the serum prior to the addition of a red cell suspension. Reaction result is expressed as the smallest amount of antigen which causes complete inhibition of hemagglutination.Hemagglutinins: Agents that cause agglutination of red blood cells. They include antibodies, blood group antigens, lectins, autoimmune factors, bacterial, viral, or parasitic blood agglutinins, etc.HN Protein: Glycoprotein from Sendai, para-influenza, Newcastle Disease, and other viruses that participates in binding the virus to cell-surface receptors. The HN protein possesses both hemagglutinin and neuraminidase activity.Reassortant Viruses: Viruses containing two or more pieces of nucleic acid (segmented genome) from different parents. Such viruses are produced in cells coinfected with different strains of a given virus.Lectins: Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.Acetamides: Derivatives of acetamide that are used as solvents, as mild irritants, and in organic synthesis.Influenza A Virus, H2N2 Subtype: A subtype of INFLUENZA A VIRUS comprised of the surface proteins hemagglutinin 2 and neuraminidase 2. The H2N2 subtype was responsible for the Asian flu pandemic of 1957.Influenza A Virus, H7N9 Subtype: A subtype of INFLUENZA A VIRUS with the surface proteins hemagglutinin 7 and neuraminidase 9. This avian origin virus was first identified in humans in 2013.Influenza A Virus, H9N2 Subtype: A subtype of INFLUENZA A VIRUS comprised of the surface proteins hemagglutinin 9 and neuraminidase 2. The H9N2 subtype usually infects domestic birds (POULTRY) but there have been some human infections reported.Dogs: The domestic dog, Canis familiaris, comprising about 400 breeds, of the carnivore family CANIDAE. They are worldwide in distribution and live in association with people. (Walker's Mammals of the World, 5th ed, p1065)Newcastle disease virus: The most well known avian paramyxovirus in the genus AVULAVIRUS and the cause of a highly infectious pneumoencephalitis in fowl. It is also reported to cause CONJUNCTIVITIS in humans. Transmission is by droplet inhalation or ingestion of contaminated water or food.Influenza Vaccines: Vaccines used to prevent infection by viruses in the family ORTHOMYXOVIRIDAE. It includes both killed and attenuated vaccines. The composition of the vaccines is changed each year in response to antigenic shifts and changes in prevalence of influenza virus strains. The vaccine is usually bivalent or trivalent, containing one or two INFLUENZAVIRUS A strains and one INFLUENZAVIRUS B strain.Clostridium perfringens: The most common etiologic agent of GAS GANGRENE. It is differentiable into several distinct types based on the distribution of twelve different toxins.Viral Proteins: Proteins found in any species of virus.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Glycoproteins: Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.Wheat Germ Agglutinins: Lectins purified from the germinating seeds of common wheat (Triticum vulgare); these bind to certain carbohydrate moieties on cell surface glycoproteins and are used to identify certain cell populations and inhibit or promote some immunological or physiological activities. There are at least two isoforms of this lectin.Parainfluenza Virus 3, Human: A species of RESPIROVIRUS frequently isolated from small children with pharyngitis, bronchitis, and pneumonia.Madin Darby Canine Kidney Cells: An epithelial cell line derived from a kidney of a normal adult female dog.Carbohydrates: The largest class of organic compounds, including STARCH; GLYCOGEN; CELLULOSE; POLYSACCHARIDES; and simple MONOSACCHARIDES. Carbohydrates are composed of carbon, hydrogen, and oxygen in a ratio of Cn(H2O)n.Hemadsorption: A phenomenon manifested by an agent or substance adhering to or being adsorbed on the surface of a red blood cell, as tuberculin can be adsorbed on red blood cells under certain conditions. (Stedman, 25th ed)Peanut Agglutinin: Lectin purified from peanuts (ARACHIS HYPOGAEA). It binds to poorly differentiated cells and terminally differentiated cells and is used in cell separation techniques.DucksBirds: Warm-blooded VERTEBRATES possessing FEATHERS and belonging to the class Aves.Cathepsin A: A carboxypeptidase that catalyzes the release of a C-terminal amino acid with a broad specificity. It also plays a role in the LYSOSOMES by protecting BETA-GALACTOSIDASE and NEURAMINIDASE from degradation. It was formerly classified as EC 3.4.12.1 and EC 3.4.21.13.Receptors, Virus: Specific molecular components of the cell capable of recognizing and interacting with a virus, and which, after binding it, are capable of generating some signal that initiates the chain of events leading to the biological response.Gangliosides: A subclass of ACIDIC GLYCOSPHINGOLIPIDS. They contain one or more sialic acid (N-ACETYLNEURAMINIC ACID) residues. Using the Svennerholm system of abbrevations, gangliosides are designated G for ganglioside, plus subscript M, D, or T for mono-, di-, or trisialo, respectively, the subscript letter being followed by a subscript arabic numeral to indicated sequence of migration in thin-layer chromatograms. (From Oxford Dictionary of Biochemistry and Molecular Biology, 1997)Viral Plaque Assay: Method for measuring viral infectivity and multiplication in CULTURED CELLS. Clear lysed areas or plaques develop as the VIRAL PARTICLES are released from the infected cells during incubation. With some VIRUSES, the cells are killed by a cytopathic effect; with others, the infected cells are not killed but can be detected by their hemadsorptive ability. Sometimes the plaque cells contain VIRAL ANTIGENS which can be measured by IMMUNOFLUORESCENCE.Cyclopentanes: A group of alicyclic hydrocarbons with the general formula R-C5H9.Glycosylation: The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.Hemagglutination Tests: Sensitive tests to measure certain antigens, antibodies, or viruses, using their ability to agglutinate certain erythrocytes. (From Stedman, 26th ed)Paramyxoviridae: A family of spherical viruses, of the order MONONEGAVIRALES, somewhat larger than the orthomyxoviruses, and containing single-stranded RNA. Subfamilies include PARAMYXOVIRINAE and PNEUMOVIRINAE.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Hymecromone: A coumarin derivative possessing properties as a spasmolytic, choleretic and light-protective agent. It is also used in ANALYTICAL CHEMISTRY TECHNIQUES for the determination of NITRIC ACID.Erythrocytes: Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN.Periodic Acid: A strong oxidizing agent.Glycoside HydrolasesEnzyme Inhibitors: Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.Mucolipidoses: A group of inherited metabolic diseases characterized by the accumulation of excessive amounts of acid mucopolysaccharides, sphingolipids, and/or glycolipids in visceral and mesenchymal cells. Abnormal amounts of sphingolipids or glycolipids are present in neural tissue. INTELLECTUAL DISABILITY and skeletal changes, most notably dysostosis multiplex, occur frequently. (From Joynt, Clinical Neurology, 1992, Ch56, pp36-7)Molecular Weight: The sum of the weight of all the atoms in a molecule.Hemagglutination: The aggregation of ERYTHROCYTES by AGGLUTININS, including antibodies, lectins, and viral proteins (HEMAGGLUTINATION, VIRAL).Antibodies, Viral: Immunoglobulins produced in response to VIRAL ANTIGENS.Arthrobacter: A genus of asporogenous bacteria isolated from soil that displays a distinctive rod-coccus growth cycle.Pandemics: Epidemics of infectious disease that have spread to many countries, often more than one continent, and usually affecting a large number of people.Amantadine: An antiviral that is used in the prophylactic or symptomatic treatment of influenza A. It is also used as an antiparkinsonian agent, to treat extrapyramidal reactions, and for postherpetic neuralgia. The mechanisms of its effects in movement disorders are not well understood but probably reflect an increase in synthesis and release of dopamine, with perhaps some inhibition of dopamine uptake.Chick Embryo: The developmental entity of a fertilized chicken egg (ZYGOTE). The developmental process begins about 24 h before the egg is laid at the BLASTODISC, a small whitish spot on the surface of the EGG YOLK. After 21 days of incubation, the embryo is fully developed before hatching.Virus Replication: The process of intracellular viral multiplication, consisting of the synthesis of PROTEINS; NUCLEIC ACIDS; and sometimes LIPIDS, and their assembly into a new infectious particle.Sialoglycoproteins: Glycoproteins which contain sialic acid as one of their carbohydrates. They are often found on or in the cell or tissue membranes and participate in a variety of biological activities.Pronase: A proteolytic enzyme obtained from Streptomyces griseus.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Trypsin: A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase: An amidohydrolase that removes intact asparagine-linked oligosaccharide chains from glycoproteins. It requires the presence of more than two amino-acid residues in the substrate for activity. This enzyme was previously listed as EC 3.2.2.18.Actinomycetaceae: A family of bacteria including numerous parasitic and pathogenic forms.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Chickens: Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.Parainfluenza Virus 1, Human: A species of RESPIROVIRUS also called hemadsorption virus 2 (HA2), which causes laryngotracheitis in humans, especially children.Isoelectric Focusing: Electrophoresis in which a pH gradient is established in a gel medium and proteins migrate until they reach the site (or focus) at which the pH is equal to their isoelectric point.Respirovirus: A genus of the family PARAMYXOVIRIDAE (subfamily PARAMYXOVIRINAE) where all the virions have both HEMAGGLUTININ and NEURAMINIDASE activities and encode a non-structural C protein. SENDAI VIRUS is the type species.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Epitopes: Sites on an antigen that interact with specific antibodies.Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase: A group of related enzymes responsible for the endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose-content glycopeptides and GLYCOPROTEINS.Oxo-Acid-Lyases: Enzymes that catalyze the cleavage of a carbon-carbon bond of a 3-hydroxy acid. (Dorland, 28th ed) EC 4.1.3.

The effects of digestive enzymes on characteristics of placental insulin receptor. Comparison of particulate and soluble receptor preparations. (1/3160)

The role of the surrounding membrane structure on the binding characteristics of the insulin receptor was studied by using several digestive enzymes. The effects observed with particulate membrane preparations are compared with those from soluble receptor preparations. beta-Galactosidase and neuraminidase had no effect on insulin binding to either particulate or soluble receptors from human placentae. Exposure to 2 units of phospholipase C/ml increased insulin binding to particulate membranes, but was without effect on the soluble receptor preparation. The increase in binding to particulate membranes was shown to be due to an increase in apparent receptor number. After 5 min exposure to 500 microgram of trypsin/ml there was an increase in insulin binding to the particulate membrane fraction, owing to an increase in receptor affinity. After 15 min exposure to this amount of trypsin, binding decreased, owing to a progressive decrease in receptor availability. In contrast, this concentration of trypsin had no effect on the solubilized receptor preparation. Because of the differential effects of phospholipase C and trypsin on the particulate compared with the solubilized receptor preparations, it is concluded that the effects of these enzymes were due to an effect on the surrounding membrane structure. Changes in receptor configuration due to alterations within the adjoining membrane provide a potential mechanism for mediating short-term alterations in receptor function.  (+info)

Cell surface sialic acid and the regulation of immune cell interactions: the neuraminidase effect reconsidered. (2/3160)

It has been known for over a decade that sialidase (neuraminidase) treatment could substantially enhance the capacity of resting B cells to stimulate the proliferation of allogeneic and antigen specific, syngeneic T cells. Thus, cell-surface sialic acid was implicated as a potential modulator of immune cell interaction. However, little progress has been made in either identifying explicit roles for sialic acid in this system or in hypothesizing mechanisms to explain the "neuraminidase effect." Here we show for the first time that cell surface sialic acid on medium incubated B cells blocks access to costimulatory molecules on the B cell surface, and that this is the most likely explanation for the neuraminidase effect. Further, we show that it is likely to be upregulation of ICAM-1 and its subsequent engagement of LFA-1 rather than loss of cell surface sialic acid that in part regulates access to CD86 and other costimulatory molecules. However, we cannot exclude a role for CD86-bound sialic acid on the B cell in modulating binding to T cell CD28. Because sialidase treatment of resting B cells but not resting T cells enables T cell activation, we suggest that sialidase treatment may still be an analogue for an authentic step in B cell activation, and show that for highly activated B cells (activated with polyclonal anti-IgM plus INF-gamma) there is specific loss 2, 6-linked sialic acid. Potential roles for sialic acid in modulating B cell/T cell collaboration are discussed.  (+info)

N-Linked glycosylation and sialylation of the acid-labile subunit. Role in complex formation with insulin-like growth factor (IGF)-binding protein-3 and the IGFs. (3/3160)

Over 75% of the circulating insulin-like growth factors (IGF-I and -II) are bound in 140-kDa ternary complexes with IGF-binding protein-3 (IGFBP-3) and the 84-86-kDa acid-labile subunit (ALS), a glycoprotein containing 20 kDa of carbohydrate. The ternary complexes regulate IGF availability to the tissues. Since interactions of glycoproteins can be influenced by their glycan moieties, this study aimed to determine the role of ALS glycosylation in ternary complex formation. Complete deglycosylation abolished the ability of ALS to associate with IGFBP-3. To examine this further, seven recombinant ALS mutants each lacking one of the seven glycan attachment sites were expressed in CHO cells. All the mutants bound IGFBP-3, demonstrating that this interaction is not dependent on any single glycan chain. Enzymatic desialylation of ALS caused a shift in isoelectric point from 4.5 toward 7, demonstrating a substantial contribution of anionic charge by sialic acid. Ionic interactions are known to be involved in the association between ALS and IGFBP-3. Desialylation reduced the affinity of ALS for IGFBP-3. IGF complexes by 50-80%. Since serum protein glycosylation is often modified in disease states, the dependence of IGF ternary complex formation on the glycosylation state of ALS suggests a novel mechanism for regulation of IGF bioavailability.  (+info)

Binding partners for the myelin-associated glycoprotein of N2A neuroblastoma cells. (4/3160)

The myelin-associated glycoprotein (MAG) has been proposed to be important for the integrity of myelinated axons. For a better understanding of the interactions involved in the binding of MAG to neuronal axons, we performed this study to identify the binding partners for MAG on neuronal cells. Experiments with glycosylation inhibitors revealed that sialylated N-glycans of glycoproteins represent the major binding sites for MAG on the neuroblastoma cell line N2A. From extracts of [3H]glucosamine-labelled N2A cells several glycoproteins with molecular weights between 20 and 230 kDa were affinity-precipitated using immobilised MAG. The interactions of these proteins with MAG were sialic acid-dependent and specific for MAG.  (+info)

Carbohydrate on human factor VIII/von Willebrand factor. Impairment of function by removal of specific galactose residues. (5/3160)

Human factor VIII/von Willebrand factor protein containing 120 +/- 12 nmol of sialic acid and 135 +/- 13 nmol of galactose/mg of protein was digested with neuraminidase. The affinity of native factor VIII/von Willebrand factor and its asialo form for the hepatic lectin that specifically binds asialoglycoproteins was assessed from in vitro binding experiments. Native factor VIII/von Willebrand factor exhibited negligible affinity while binding of the asialo derivative was comparable to that observed for asialo-alpha1-acid glycoprotein. Incubation of asialo-factor VIII/von Willebrand factor with Streptococcus pneumoniae beta-galactosidase removed only 62% of the galactose but abolished binding to the purified hepatic lectin. When the asialo derivative was incubated with purified beta-D-galactoside alpha2 leads to 6 sialyltransferase and CMP-[14C]NeuAc, only 61% of the galactose incorporated [14C]NeuAc. From the known specificites of these enzymes, it is concluded that galactose residues important in lectin binding are present in a terminal Gal/beta1 leads to 4GlcNAc sequence on asialo-factor VIII/von Willebrand factor. The relative ristocetin-induced platelet aggregating activity of native, asialo-, and agalacto-factor VIII/von Willebrand factor was 100:38:12, respectively, while procoagulant activity was 100:100:103.  (+info)

Tandem amino acid repeats from Trypanosoma cruzi shed antigens increase the half-life of proteins in blood. (6/3160)

Proteins containing amino acid repeats are widespread among protozoan parasites. It has been suggested that these repetitive structures act as immunomodulators, but other functional aspects may be of primary importance. We have recently suggested that tandem repeats present in Trypanosoma cruzi trans-sialidase stabilize the catalytic activity in blood. Because the parasite releases trans-sialidase, this delayed clearance of the enzyme might have implications in vivo. In the present work, the ability of repetitive units from different T. cruzi molecules in stabilizing trans-sialidase activity in blood was evaluated. It is shown that repeats present on T. cruzi shed proteins (antigens 13 and Shed-Acute-Phase-Antigen [SAPA]) increase trans-sialidase half-life in blood from 7 to almost 35 hours. Conversely, those repeats present in intracellular T. cruzi proteins only increase the enzyme half-life in blood up to 15 hours. Despite these results, comparative analysis of structural and catalytic properties of both groups of chimeric enzymes show no substantial differences. Interestingly, antigens 13 and SAPA also increase the persistence in blood of chimeric glutathione S-transferases, thus suggesting that this effect is inherent to these repeats and independent of the carrier protein. Although the molecular basis of this phenomenon is still uncertain, its biotechnological potential can be envisaged.  (+info)

Amino acid substitutions in a conserved region in the stalk of the Newcastle disease virus HN glycoprotein spike impair its neuraminidase activity in the globular domain. (7/3160)

The ectodomain of the paramyxovirus haemagglutinin-neuraminidase (HN) glycoprotein spike can be divided into two regions: a membrane-proximal, stalk-like structure and a terminal globular domain. The latter contains all the antibody recognition sites of the protein, as well as its receptor recognition and neuraminidase (NA) active sites. These two activities of the protein can be separated by monoclonal antibody functional inhibition studies and mutations in the globular domain. Herein, we show that mutation of several conserved residues in the stalk of the Newcastle disease virus HN protein markedly decrease its NA activity without a significant effect on receptor recognition. Thus, mutations in the stalk, distant from the NA active site in the globular domain, can also separate attachment and NA. These results add to an increasing body of evidence that the NA activity of this protein is dependent on an intact stalk structure.  (+info)

Ortho- and paramyxoviruses from migrating feral ducks: characterization of a new group of influenza A viruses. (8/3160)

Ortho- and parainfluenza viruses isolated from the cloacas of migrating feral ducks shot on the Mississippi flyway included three strains of influenza. A virus (Hav6 Nav1, Hav6 Nl, Hav7 Neq2) as well as Newcastle disease virus. One influenza virus, A/duck/Memphis/546/74, possessed Hav3 haemagglutinin, but the neuraminidase was not inhibited by any of the known influenza reference antisera. The neuraminidase on this virus was related to the neuraminidases on A/duck/GDR/72 (H2 N?), A/turkey/Ontario/7732/66 (Hav 5 N?), A/duck/Ukraine/1/60 (Hav3 N?) and A/turkey/Wisconsin/68. We therefore propose that the neuraminidase on this group of influenza viruses be designated Nav6. The A/duck/Memphis/546/74 influenza virus caused an ocular discharge in 1 of 5 ducks and was shed in faeces for 10 days; it was stable in faecal samples for up to 3 days at 20 degrees C. These results suggest that ecological studies on influenza in avian species should include attempts to isolate virus from faeces. Faecal-oral transmission is an attractive explanation for the spread of influenza virus from feral birds to other animals.  (+info)

Bacterial neuraminidase - WikipediaBacterial neuraminidase - Wikipedia
Bacterial neuraminidase is type of neuraminidase and a virulence factor for many bacteria including Bacteroides fragilis and Pseudomonas aeruginosa. Its function is to cleave a sialic acid residue off ganglioside-GM1 (a modulator of cell surface and receptor activity) turning it into asialo-GM1 to which type 4 pilli (attachment factors) bind preferentially. Gaskell A, Crennell S, Taylor G (November 1995). "The three domains of a bacterial sialidase: a beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll". Structure. 3 (11): 1197-205. doi:10.1016/s0969-2126(01)00255-6. PMID 8591030. Molecular and Cellular Biology ...
Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding. | Journal of...Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding. | Journal of...
We have used a neuraminidase-deficient influenza virus, NWS-Mvi, which was selected by supplying bacterial neuraminidase in the medium (C. Liu and G. M. Air, Virology 194:403-407, 1993), to define the role of neuraminidase in influenza virus replication. Electron microscopy showed that virions of the NWS-Mvi mutant assembled normally and formed large aggregates associated with cell surfaces. The NWS-Mvi virus grown in the absence of neuraminidase was able to carry out a second round of replication in MDCK cells without added neuraminidase, indicating that the virus particles contained in these aggregates were infectious. Aggregates of virus were also found in cytoplasmic vacuoles. When virus-infected cells were incubated in the presence of ferritin, such aggregates were found to be labeled with ferritin, indicating that they are derived from uptake at the cell surface. When the neuraminidase-deficient virus was administered intranasally to C57BL/6 mice, low titers of virus were recovered from ...
Influenza Virus Sialidase - A Drug Discovery TargetInfluenza Virus Sialidase - A Drug Discovery Target
Influenza continues to be an ongoing problem despite the existence of vaccines and drugs. Disease outbreaks can occur relatively quickly as witnessed with the recent emergence of the influenza virus A/H1N1 pandemic. The development of new anti-influenza drugs is thus a major challenge. This volume describes all aspects of the virus structure and function relevant to infection. The focus is on drug discovery of inhibitors to the enzyme sialidase, which plays a key role in the infectious lifecycle of the virus. Following an overview of the influenza virus, the haemagglutinin, the interactions with the cell receptors and the enzymology of virus sialidase, recent results in drug design are presented. These include a full coverage of the design, synthesis and evaluation of carbohydrate as well as non-carbohydrate influenza virus sialidase inhibitors. Further reviews of the clinical experience with influenza virus sialidase inhibitors and of the development of resistance to these inhibitor drugs ...
Anti-Influenza B Virus Neuraminidase Antibody | Mouse Monoclonal | LSBioAnti-Influenza B Virus Neuraminidase Antibody | Mouse Monoclonal | LSBio
Influenza B Virus Neuraminidase antibody LS-C83326 is an unconjugated mouse monoclonal antibody to influenza virus Influenza B Virus Neuraminidase. Validated for Inhb.
RCSB PDB - 2C4A: STRUCTURE OF NEURAMINIDASE SUBTYPE N9 COMPLEXED WITH 30 MM SIALIC ACID (NANA, NEU5AC), CRYSTAL SOAKED FOR 3...RCSB PDB - 2C4A: STRUCTURE OF NEURAMINIDASE SUBTYPE N9 COMPLEXED WITH 30 MM SIALIC ACID (NANA, NEU5AC), CRYSTAL SOAKED FOR 3...
2C4A: STRUCTURE OF NEURAMINIDASE SUBTYPE N9 COMPLEXED WITH 30 MM SIALIC ACID (NANA, NEU5AC), CRYSTAL SOAKED FOR 3 HOURS AT 291 K.
Welcome to CDC stacks | Neuraminidase Inhibitor Susceptibility Testing in Human Influenza Viruses: A Laboratory Surveillance...Welcome to CDC stacks | Neuraminidase Inhibitor Susceptibility Testing in Human Influenza Viruses: A Laboratory Surveillance...
Neuraminidase inhibitors (NAIs) are vital in managing seasonal and pandemic influenza infections. NAI susceptibilities of virus isolates (n = 5540) collected during the 2008-2009 influenza season were assessed in the chemiluminescent neuraminidase inhibition (NI) assay. Box-and-whisker plot analyses of log-transformed IC(50)s were performed for each virus type/subtype and NAI to identify outliers which were characterized based on a statistical cutoff of IC(50) >3 interquartile ranges (IQR) from the 75(th) percentile. Among 1533 seasonal H1N1 viruses tested, 1431 (93.3%) were outliers for oseltamivir; they all harbored the H275Y mutation in the neuraminidase (NA) and were reported as oseltamivir-resistant. Only 15 (0.7%) of pandemic 2009 H1N1 viruses tested (n = 2259) were resistant to oseltamivir. All influenza A(H3N2) (n = 834) and B (n = 914) viruses were sensitive to oseltamivir, except for one A(H3N2) and one B virus, with D151V and D197E (D198E in N2 numbering) mutations in the NA, ...
The cytosolic sialidase Neu2 is degraded by autophagy during myoblast atrophy - Institutional Repository University of AntwerpThe cytosolic sialidase Neu2 is degraded by autophagy during myoblast atrophy - Institutional Repository University of Antwerp
Background The sialidase Neu2 is a cytosolic enzyme which is fully expressed in mature muscle myofibers. Methods To investigate Neu2 expression during muscle atrophy, we employed an in vitro model consisting of terminally differentiated C2C12 myotubes exposed to different pro-atrophic stimuli that triggered catabolic pathways involved in proteasome activation or autophagy. Results Neu2 expression was unchanged in myotubes treated with TNF-alpha, a cytokine known to activate the proteasome. However, Neu2 transcript levels and enzymatic activity were downregulated in starved or dexamethasone-treated myotubes that showed proteosomal activation and several hallmarks of macroautophagy, such as formation of autophagosomes, the accumulation of LC3 dots and bulk degradation of long-lived proteins. Neu2 activity and protein levels were rescued upon cotreatment with the lysosomotropic agent NH4Cl, the autophagy inhibitor 3-methyladenine or cathepsin inhibitors, as well as by insulin administration, but ...
RCSB PDB - 1A14: COMPLEX BETWEEN NC10 ANTI-INFLUENZA VIRUS NEURAMINIDASE SINGLE CHAIN ANTIBODY WITH A 5 RESIDUE LINKER AND...RCSB PDB - 1A14: COMPLEX BETWEEN NC10 ANTI-INFLUENZA VIRUS NEURAMINIDASE SINGLE CHAIN ANTIBODY WITH A 5 RESIDUE LINKER AND...
1A14: COMPLEX BETWEEN NC10 ANTI-INFLUENZA VIRUS NEURAMINIDASE SINGLE CHAIN ANTIBODY WITH A 5 RESIDUE LINKER AND INFLUENZA VIRUS NEURAMINIDASE
British Library EThOS: Structure and function of a neuraminidase from Streptococcus pneumoniaeBritish Library EThOS: Structure and function of a neuraminidase from Streptococcus pneumoniae
The aim of this project was to characterise a neuraminidase from Streptococcus pneumoniae by relating its amino acid sequence to the enzymatic activity of the protein, leading to the production of mutated neuraminidases that could be tested as protective immunogens. The sequence of the cloned neuraminidase gene (nan A), was compared to other bacterial neuraminidases to identify conserved residues, and also utilising crystallography data, predictions were made of the residues likely to be important in catalysis. Three residues, glutamic acid (E) 647, arginine (R) 663 and tyrosine (Y) 752 were chosen for further study. To assess the importance of these residues in catalysis, conservative substitutions of these residues (E647 > Q, R663 > H and Y752 > F) were made and the subsequent effect of enzyme activity measured. The wild-type and mutated neuraminidase genes were cloned into the expression vector pQE30 and purified by Ni-NTA affinity chromatography. The purified neuraminidases were assayed for ...
JCI - Bacterial neuraminidase facilitates mucosal infection by participating in biofilm productionJCI - Bacterial neuraminidase facilitates mucosal infection by participating in biofilm production
Many respiratory pathogens, including Hemophilus influenzae, Streptococcus pneumoniae, and Pseudomonas aeruginosa, express neuraminidases that can cleave α2,3-linked sialic acids from glycoconjugates. As mucosal surfaces are heavily sialylated, neuraminidases have been thought to modify epithelial cells by exposing potential bacterial receptors. However, in contrast to neuraminidase produced by the influenza virus, a role for bacterial neuraminidase in pathogenesis has not yet been clearly established. We constructed a mutant of P. aeruginosa PAO1 by deleting the PA2794 neuraminidase locus (Δ2794) and tested its virulence and immunostimulatory capabilities in a mouse model of infection. Although fully virulent when introduced i.p., the Δ2794 mutant was unable to establish respiratory infection by i.n. inoculation. The inability to colonize the respiratory tract correlated with diminished production of biofilm, as assessed by scanning electron microscopy and in vitro assays. The importance of ...
Recombinant H7N9 Neuraminidase/NA Protein, HEK293 Cells, 40108-VNAHC | Sino BiologicalRecombinant H7N9 Neuraminidase/NA Protein, HEK293 Cells, 40108-VNAHC | Sino Biological
Recombinant H7N9 Neuraminidase/NA Protein (His36-Leu465) 40108-VNAHC is expressed in HEK293 Cells. With high purity, high biological activity, high stability, and other superior features, you can use this H7N9 Neuraminidase/NA protein for relevant bioassay and related research.
In vitro evaluation of neuraminidase inhibitors using the neuraminidase-dependent release assay of hemagglutinin-pseudotyped...In vitro evaluation of neuraminidase inhibitors using the neuraminidase-dependent release assay of hemagglutinin-pseudotyped...
For the treatment of influenza virus infections, neuraminidase inhibitors (NAIs) that prevent the release of virus particles have been effective against most influenza strains. Several neuraminidase (NA) assays are available for the evaluation of NAIs. To understand the NAI functions under physiological conditions, assays mimicking viral particle release should be useful. We have constructed retrovirus-based reporter viruses that are pseudotyped with hemagglutinin (HA) glycoprotein by transfection of producer cells using plasmids expressing retroviral gag-pol, influenza HA, NA, and firefly luciferase genes. Similarly to the life cycle of influenza viruses, the release of pseudotype viruses also requires neuraminidase functions. This requirement was used to develop an assay to evaluate NAI activities by measuring inhibition of pseudotype virus production at different NAI concentrations. The pseudotype virus release assay was used to determine the IC(50) values of Oseltamivir carboxylate, ...
Inhibition of Neuraminidase Inhibitor-Resistant Influenza Virus by DAS181, a Novel Sialidase Fusion ProteinInhibition of Neuraminidase Inhibitor-Resistant Influenza Virus by DAS181, a Novel Sialidase Fusion Protein
Antiviral drug resistance for influenza therapies remains a concern due to the high prevalence of H1N1 2009 seasonal influenza isolates which display H274Y associated oseltamivir-resistance. Furthermore, the emergence of novel H1N1 raises the potential that additional reassortments can occur, resulting in drug resistant virus. Thus, additional antiviral approaches are urgently needed. DAS181 (Fludase®), a sialidase fusion protein, has been shown to have inhibitory activity against a large number of seasonal influenza strains and a highly pathogenic avian influenza (HPAI) strain (H5N1). Here, we examine the in vitro activity of DAS181 against a panel of 2009 oseltamivir-resistant seasonal H1N1 clinical isolates. The activity of DAS181 against nine 2009, two 2007, and two 2004 clinical isolates of seasonal IFV H1N1 was examined using plaque number reduction assay on MDCK cells. DAS181 strongly inhibited all tested isolates. EC50 values remained constant against isolates from 2004, 2007, and 2009,
Anti-Swine H1N1 Neuraminidase antibody (ab91643) ProtocolsAnti-Swine H1N1 Neuraminidase antibody (ab91643) Protocols
There are no specific protocols for Anti-Swine H1N1 Neuraminidase antibody (ab91643). Please download our general protocols booklet
Neuraminidase is important for the initiation of influenza virus infection in human airway epitheliumNeuraminidase is important for the initiation of influenza virus infection in human airway epithelium
Influenza virus neuraminidase (NA) plays an essential role in release and spread of progeny virions, following the intracellular viral replication cycle. To test whether NA could also facilitate virus entry into cell, we infected cultures of human airway epithelium with human and avian influenza viruses in the presence of the NA inhibitor oseltamivir carboxylate. Twenty- to 500-fold less cells became infected in drug-treated versus nontreated cultures (P , 0.0001) 7 h after virus application, indicating that the drug suppressed the initiation of infection. These data demonstrate that viral NA plays a role early in infection, and they provide further rationale for the prophylactic use of NA inhibitors ...
1snt - Proteopedia, life in 3D1snt - Proteopedia, life in 3D
Gangliosides play key roles in cell differentiation, cell-cell interactions, and transmembrane signaling. Sialidases hydrolyze sialic acids to produce asialo compounds, which is the first step of degradation processes of glycoproteins and gangliosides. Sialidase involvement has been implicated in some lysosomal storage disorders such as sialidosis and galactosialidosis. Neu2 is a recently identified human cytosolic sialidase. Here we report the first high resolution x-ray structures of mammalian sialidase, human Neu2, in its apo form and in complex with an inhibitor, 2-deoxy-2,3-dehydro-N-acetylneuraminic acid (DANA). The structure shows the canonical six-blade beta-propeller observed in viral and bacterial sialidases with its active site in a shallow crevice. In the complex structure, the inhibitor lies in the catalytic crevice surrounded by ten amino acids. In particular, the arginine triad, conserved among sialidases, aids in the proper positioning of the carboxylate group of DANA within the ...
X-NeuNAc | X-Neu5Ac | CB-1339 | CAS#160369-85-7 | Neuraminidase Substrate | MedKooX-NeuNAc | X-Neu5Ac | CB-1339 | CAS#160369-85-7 | Neuraminidase Substrate | MedKoo
X-NeuNAc, also known as CB1339 and X-Neu5Ac, is a novel substrate for chromogenic assay of neuraminidase activity in bacterial expression systems. X-NeuNAc can be used to facilitate the screening of bacterial colonies or plaques for the detection of either natural or mutant neuraminidase activity. Preliminary kinetic studies indicate that this compound is a good substrate (Km 0.89 x 10(-3) M) for neuraminidase and is quite stable under identical conditions in the absence of enzyme. These results suggest that X-Neu5Ac can be useful to screen for bacterially-encoded enzyme production directly on agar plates.
Autoimmune Reactions Against Liver Cells by Syngeneic Neuraminidase-Treated Lymphocytes | The Journal of ImmunologyAutoimmune Reactions Against Liver Cells by Syngeneic Neuraminidase-Treated Lymphocytes | The Journal of Immunology
We have found that the entrapment of neuraminidase-treated lymphocytes in the liver leads to the induction of autoimmune cellular cytotoxic reactions.. Lymphocytes from mouse spleen and thymus were incubated with neuraminidase in vitro and injected i.v. into syngeneic recipients. Lymphocytic infiltrations into the liver were seen 7 days later with both types of cells. After repeated weekly injections of asialo-lymphocytes, destruction of liver tissue became apparent. Electronmicroscopic studies showed that hepatocytes, fat storage cells, and endothelial cells were affected, mainly at the hepatic periphery.. It is concluded that the adhesion of asialo-lymphocytes to liver cells induces their cytotoxic activity. Similar reactions may occur after paramyxovirus infection due to the action of viral neuraminidase.. ...
Further studies on the effect of neuraminidase on tumor cell transpla by B H. Sanford and J F. CodingtonFurther studies on the effect of neuraminidase on tumor cell transpla" by B H. Sanford and J F. Codington
Adenocarcinoma, Animal, Ascitic-Fluid: cy, Binding-Sites-Antibody, Cells-Cultured, Complement, Cytotoxicity-Tests-Immunologic, Female, Male, Mammary-Neoplasms-Experimental, Mice, Neoplasm-Transplantation, Neuraminic-Acids: an, Neuraminidase, Vibrio: en. ...
Antigenic drift - WikipediaAntigenic drift - Wikipedia
In the influenza virus, the two relevant antigens are the surface proteins, hemagglutinin and neuraminidase.[4] The hemagglutinin is responsible for binding and entry into host epithelial cells while the neuraminidase is involved in the process of new virions budding out of host cells.[5] Sites recognized on the hemagglutinin and neuraminidase proteins by host immune systems are under constant selective pressure. Antigenic drift allows for evasion of these host immune systems by small mutations in the hemagglutinin and neuraminidase genes that make the protein unrecognizable to pre-existing host immunity.[6] Antigenic drift is this continuous process of genetic and antigenic change among flu strains.[7]. In human populations, immune (vaccinated) individuals exert selective pressure for single point mutations in the hemagglutinin gene that increase receptor binding avidity, while naive individuals exert selective pressure for single point mutations that decrease receptor binding avidity.[6] These ...
Recognition of the PB1, neuraminidase, and matrix proteins of influenza virus A/NT/60/68 by cytotoxic T lymphocytes. - NDM...Recognition of the PB1, neuraminidase, and matrix proteins of influenza virus A/NT/60/68 by cytotoxic T lymphocytes. - NDM...
We have investigated the recognition of the PB1, neuraminidase, and matrix (M1) proteins of influenza virus A/NT/60/68 (H3N2 subtype) by secondary in vitro stimulated polyclonal cytotoxic T lymphocyte (CTL) populations. While these three proteins have different functions and cellular locations, they can all be recognized as target antigens. However, the immunogenicity of these proteins for CTLs is under strict genetic control. Thus, PB1 protein is recognized as a cross-reactive target antigen by CTLs raised in CBA (H-2k) but not BALB/c (H-2d) mice. CBA, but not BALB/c mice, also generate a low-level CTL response to the neuraminidase. This latter response was only detectable following in vivo priming of CBA mice with a recombinant vaccinia virus expressing neuraminidase (N2-VACC). The matrix protein, expressed from recombinant vaccinia virus M-VACC, was not recognized as an antigen by CTL generated from either CBA or BALB/c strains of mice. By contrast, human HLA-A2-restricted influenza virus-specific
Cutting through mucus with the influenza virus neuraminidaseCutting through mucus with the influenza virus neuraminidase
The influenza virus NA, which is important for virus release from cells, also aids in infection by degrading the mucus barrier of the respiratory tract.
JCI - Bacterial neuraminidase facilitates mucosal infection by participating in biofilm productionJCI - Bacterial neuraminidase facilitates mucosal infection by participating in biofilm production
Construction of a P. aeruginosa PAO1 neuraminidase null mutant A nanA null mutant (Δ2794) was constructed by allelic replacement. An in-frame nonpolar deletion allele was constructed by removing the nanA coding sequence corresponding to amino acids 5-435 of the predicted 438-residue polypeptide and used to replace the full-length gene (1,317 base pairs) by the method previously described (56). Primers were designed using the published DNA sequence for the neuraminidase gene (designated PA2794) from P. aeruginosa strain PAO1 (GenBank accession no. AF236853). A nanA complementation plasmid was constructed by cloning a PCR product corresponding to the full-length neuraminidase open reading frame into plasmid pMMBGW with either a gentamicin or a penicillin resistance marker (56). The complementation clone or an empty vector control was introduced into the Δ2794 mutant by conjugation and selection on gentamicin (40 μg/ml) or piperacillin (100 μg/ml). The same procedure was carried out to generate ...
Health News Med: Drug Information Update - FDA approves Rapivab to treat flu infectionHealth News Med: Drug Information Update - FDA approves Rapivab to treat flu infection
On December 19, the U.S. Food and Drug Administration approved Rapivab (peramivir) to treat influenza infection in adults.. Influenza, commonly known as the flu, is a contagious respiratory illness caused by influenza viruses. Flu infections can range from mild to severe and can sometimes lead to hospitalization and death. According to the Centers for Disease Control and Prevention (CDC), 5-20 percent of the American population gets the flu and more than 200,000 people are hospitalized from seasonal flu-related complications each year.. Rapivab is an inhibitor of influenza virus neuraminidase, an enzyme that releases viral particles from infected cells. Neuraminidase inhibitors are commonly used to treat flu infection. Rapivab is the first neuraminidase inhibitor approved for intravenous (IV) administration and is administered as a single IV dose. It is intended for patients 18 years and older who have acute uncomplicated influenza and have shown symptoms of flu for no more than two days.. For ...
Optimal conditions for the assay of fibroblast neuraminidase with different natural substrates<...Optimal conditions for the assay of fibroblast neuraminidase with different natural substrates<...
TY - JOUR. T1 - Optimal conditions for the assay of fibroblast neuraminidase with different natural substrates. AU - Caimi, L.. AU - Lombardo, A.. AU - Preti, A.. AU - Wiesmann, U.. AU - Tettamanti, G.. PY - 1979/11/9. Y1 - 1979/11/9. N2 - A method for the assay of neuraminidase in human cultured fibroblasts has been worked out. The substrates, all naturally occurring, were: sialyloligosaccharides (α(2 → 3)sialyllactose, α(2 → 6)sialyllactose, disialyllactose), sialylglycolipids (disialogangliosides GD1a and GD1b), sialylglycoproteins and sialylglycopeptides (ovine submaxillary glycoprotein and its pronase-glycopeptides). The method was based on the determination of the enzymically liberated N-acetylneuraminic acid (NeuAc) by a chromatographic-colorimetric microprocedure. The enzyme acted on sialyloligosaccharides and, in the presence of Triton X-100, on gangliosides, while it did not appreciably affect sialylglycoproteins and sialylglycopeptides. The optimum pH was 4.0 for all tested ...
Changing influenza virus neuraminidase into a receptor binding proteinChanging influenza virus neuraminidase into a receptor binding protein
Influenza viruses have been identified with NA molecules that serve as receptor binding proteins, a function usually reserved for the HA glycoprotein.
Applications filed at Oct 26 2017 | A POTENT ANTI-INFLUENZA A NEURAMINIDASE SUBTYPE N1 ANTIBODY | Patents.comApplications filed at Oct 26 2017 | A POTENT ANTI-INFLUENZA A NEURAMINIDASE SUBTYPE N1 ANTIBODY | Patents.com
CHIMERIZATION AND CHARACTERIZATION OF A MONOCLONAL ANTIBODY WITH POTENT NEUTRALIZING ACTIVITY ACROSS MULTIPLE... | METHOD FOR DETERMINING DELETIONS IN HBV PRE-S2 REGION | CELL CULTURE MEDIUM | MODIFIED PIGMENT EPITHELIUM-DERIVED FACTOR (PEDF) PEPTIDES AND USES THEREOF FOR TREATING NEOVASCULAR DISEASES,... | EGFR and C-Met Fibronectin Type III Domain Binding Molecules |
Avian Influenza A Neuraminidase抗体(ab21305)|Anti-Avian Influenza A Neuraminidase抗体Avian Influenza A Neuraminidase抗体(ab21305)|Anti-Avian Influenza A Neuraminidase抗体
Avian Influenza A Neuraminidase兔多克隆抗体(ab21305)经ELISA实验严格验证，被7篇文献引用。所有产品均提供质保服务，中国75%以上现货。
2htw - Proteopedia, life in 3D2htw - Proteopedia, life in 3D
The worldwide spread of H5N1 avian influenza has raised concerns that this virus might acquire the ability to pass readily among humans and cause a pandemic. Two anti-influenza drugs currently being used to treat infected patients are oseltamivir (Tamiflu) and zanamivir (Relenza), both of which target the neuraminidase enzyme of the virus. Reports of the emergence of drug resistance make the development of new anti-influenza molecules a priority. Neuraminidases from influenza type A viruses form two genetically distinct groups: group-1 contains the N1 neuraminidase of the H5N1 avian virus and group-2 contains the N2 and N9 enzymes used for the structure-based design of current drugs. Here we show by X-ray crystallography that these two groups are structurally distinct. Group-1 neuraminidases contain a cavity adjacent to their active sites that closes on ligand binding. Our analysis suggests that it may be possible to exploit the size and location of the group-1 cavity to develop new ...
R292K Substitution and Drug Susceptibility of Influenza A(H7N9) VirusesR292K Substitution and Drug Susceptibility of Influenza A(H7N9) Viruses
Neuraminidase inhibitors are the only licensed antiviral medications available to treat avian influenza A(H7N9) virus infections in humans. According to a neuraminidase inhibition assay, an R292K substitution reduced antiviral efficacy of inhibitors, especially oseltamivir, and decreased viral fitness in cell culture. Monitoring emergence of R292K-carrying viruses using a pH-modified neuraminidase inhibition assay should be considered.
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The Y155H amino acid substitution in the neuraminidase gene (NA) has previously been associated with highly reduced inhibition by neuraminidase inhibitors in the seasonal H1N1 influenza A virus which circulated in humans before the 2009 pandemic. During the 2012/13 epidemic season in Spain, two A(H1N1)pdm09 viruses bearing the specific Y155H substitution in the NA were detected and isolated from two patients diagnosed with severe respiratory syndrome and pneumonia requiring admission to the intensive care unit. Contrary to what was observed in the seasonal A(H1N1) viruses, neither of the Y155H A(H1N1)pdm09 viruses described here showed a phenotype of reduced inhibition by NAIs as determined by the neuraminidase enzyme inhibition assay (MUNANA). High-throughput sequencing of the NA of both Y155H viruses showed that they were composed to >99% of H155 variants. We believe that this report can contribute to a better understanding of the biological significance of amino acid substitutions in the
BCX-1812 (RWJ-270201): discovery of a novel, highly potent, orally active, and selective influenza neuraminidase inhibitor...BCX-1812 (RWJ-270201): discovery of a novel, highly potent, orally active, and selective influenza neuraminidase inhibitor...
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
Neuraminidase - BP941 | acris-antibodies.comNeuraminidase - BP941 | acris-antibodies.com
Neuraminidase, 1 ml. Neuraminidases or sialidases are exoglycosidases that catalyze the cleavage of a glycosidically linked terminal N acetyl neuraminic acid from sialylated glycoconjugates.
CAZy - CBM40CAZy - CBM40
Modules of approx. 200 residues, found at the N-terminus of GH33 sialidases. Can also be found inserted in the β-propeller of GH33 sialidases. The sialic acid binding function has been demonstrated for the N-terminal CBM40 of Vibrio cholerae sialidase (Moustafa et al. (2004) J Biol Chem 279:40819-26) (PMID: 15226294 ...
micrographs Archives - B. Thomas Photo Researchmicrographs Archives - B. Thomas Photo Research
All Images are for Editorial Use Only). This negatively-stained transmission electron micrograph (TEM) revealed the presence of a number of Hong Kong flu virus virions, the H3N2 subtype of the influenza A virus. This virus is a Orthomyxoviridae virus family member, and was responsible for the flu pandemic of 1968-1969, which infected an estimated 50,000,000 people in the United States, killing 33,000. Note the proteinaceous coat, or capsid, surroundind each virion, and the hemagglutinin-neuraminidase spikes, which differ in terms of their molecular make-up from strain to strain.. There are many different subtypes of type A influenza viruses. These subtypes differ because of changes in certain proteins on the surface of the influenza A virus (hemagglutinin [HA] and neuraminidase [NA] proteins). There are 16 known HA subtypes and 9 known NA subtypes of influenza A viruses. Many different combinations of HA and NA proteins are possible. Each combination represents a different subtype. All known ...
Avian Influenza A Neuraminidase肽(ab39804)|Abcam中国Avian Influenza A Neuraminidase肽(ab39804)|Abcam中国
购买我们的Avian Influenza A Neuraminidase肽。ab39804可作为ab21304的封闭肽并经过Blocking, ELISA实验验证。Abcam提供免费的实验方案，操作技巧及专业的支持。
NEU1 neuraminidase 1 [Homo sapiens (human)] - Gene - NCBINEU1 neuraminidase 1 [Homo sapiens (human)] - Gene - NCBI
The protein encoded by this gene is a lysosomal enzyme that cleaves terminal sialic acid residues from substrates such as glycoproteins and glycolipids. In the lysosome, this enzyme is part of a heterotrimeric complex together with beta-galactosidase and cathepsin A (the latter is also referred to as protective protein). Mutations in this gene can lead to sialidosis, a lysosomal storage disease that can be type 1 (cherry red spot-myoclonus syndrome or normosomatic type), which is late-onset, or type 2 (the dysmorphic type), which occurs at an earlier age with increased severity. [provided by RefSeq, Jul 2008 ...
Neuraminidase (Isoenzyme S), 1U - EY Laboratories, Inc.Neuraminidase (Isoenzyme S), 1U - EY Laboratories, Inc.
[button size=small text=MSDS & Datasheet link=/wp-content/uploads/media/BCDatasheets_C_10.26/E & EC/EC-32118-S.pdf]Neuraminidase (Isoenzyme S), 1
Enzymes & KinaseEnzymes & Kinase
Enzymes are indispensable for signal transduction and cell regulation, often via kinases and phosphatases. Viruses can also contain enzymes for infecting cells, such as the HIV integrase and reverse transcriptase, or for viral release from cells, like the influenza virus neuraminidase. Protease, also called proteinase, peptidase, or proteolytic enzyme, is any enzyme that performs proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in a polypeptide chain. Proteases have evolved to perform these reactions by numerous different mechanisms. Kinase is an enzyme that catalyzes the transfer of phosphate groups from high-energy, phosphate-donating molecules to specific substrates. Kinases are critical in metabolism, cell signalling, protein regulation, cellular transport, secretory processes, and many other cellular pathways. ...
Nova tehnika določevanja lokacije sladkorjev vezanih na proteine, utira pot odkritjem v medicini - Wiki FKKTNova tehnika določevanja lokacije sladkorjev vezanih na proteine, utira pot odkritjem v medicini - Wiki FKKT
Glikoproteini so proteini, na katere so kovalentno vezane sladkorne komponente. Kam na protein se le-te vežejo pa ima pomembno vlogo pri spoznavanju bolezni (katere funkcije opravljajo proteini tekom razvoja ali v različnih bolezenskih stanjih) in v razvoju novih biomarkerjev ter zdravil. Sladkorne komponente so na protein lahko N-vezane (glikozidna vez se vzpostavi med sladkorno verigo in NH2- skupino asparagina) ali O-vezane (glikozidna vez se vzpostavi med sladkorno verigo in OH- skupino serina ali treonina) slika1. Do nedavnega so morali raziskovalci za določitev, kje na proteinu je glikozilacijsko mesto, poleg masne spektrometrije, uporabiti več metod. Po zaslugi nove tehnike priprave proteinskega vzorca, za izboljšanje metode masne spektrometrije, ki je bila objavljena v reviji Nature Methods, pa je to mogoče v enem koraku. Nova tehnika priprave vzorca, narekuje selektivno oksidacijo glikoproteinov, ki imajo na prostem koncu sladkorne verige sialično kislino slika2, njihovo vezavo ...
NA Protein Degradation 2020] E3scan™ Ligand Binding Assay Platform for Targeted Protein Degradation and PROTAC® DiscoveryNA Protein Degradation 2020] E3scan™ Ligand Binding Assay Platform for Targeted Protein Degradation and PROTAC® Discovery
Regulation of immune responses is tightly controlled through a balance of co-stimulatory and inhibitory checkpoint receptors, often exploited by many cancers. Therefore, therapeutics that block inhibitory receptors or activate immuno-stimulatory checkpoint receptors have proved to be powerful agents to restore anti-tumor immune responses. However, developing drugs targeting these checkpoint proteins has proved to be quite challenging, as cell-based assays used to screen for functional drugs are often difficult to create, involve the use of human primary cells, and have long, complicated protocols. Here, we present data for the new PathHunter® Checkpoint assays that target clinically relevant co-inhibitory and co-stimulatory checkpoint receptors and measure receptor activation and signaling, using the industry-validated Enzyme Fragment Complementation (EFC) technology. These assays facilitate the development of relevant therapeutics, enabling rapid and sensitive screening of biologics and small ...
Active ConstituentActive Constituent
Yu, M., Wang, Y., Tian, L., Wang, Y., Wang, X., Liang, W., . . . Fang, X. (2015). Safflomin A inhibits neuraminidase activity and influenza virus replication. RSC Adv., 5(114), 94053-94066. doi:10.1039/c5ra17336a ...
sialidase - oisialidase - oi
EC 3.2.1.18; recommended name: exo‐α‐sialidase; former name: neuraminidase; a glycosidase enzyme that hydrolyses 2,3‐, 2,6‐, and 2,8‐glucosidic linkages joining terminal nonreducing N‐ or O‐acylneuraminyl residues to galactose, N‐acetylhexosamine, or N‐ or O‐acylated neuraminyl residues in oligosaccharides, glycoproteins, or glycolipids.. [...] ...
virus na Saraivavirus na Saraiva
Encontre virus com ótimos preços e condições na Saraiva. Temos A História da Humanidade Contada Pelos Vírus, Zika Virus Disease - From Origin To Outbreak e muito mais.
CAZy - GH33CAZy - GH33
sialidase or neuraminidase (EC 3.2.1.18); trans-sialidase (EC 2.4.1.-); anhydrosialidase (EC 4.2.2.15); Kdo hydrolase (EC 3.2.1.-); 2-keto-3-deoxynononic acid hydrolase / KDNase (EC 3.2.1.- ...
A RADIOMETRIC ASSAY FOR GANGLIOSIDE SIALIDASE APPLIED TO THE DETERMINATION OF THE ENZYME SUBCELLULAR LOCATION IN CULTURED HUMAN...A RADIOMETRIC ASSAY FOR GANGLIOSIDE SIALIDASE APPLIED TO THE DETERMINATION OF THE ENZYME SUBCELLULAR LOCATION IN CULTURED HUMAN...
A radiometric method for the assay of ganglioside sialidase in cultured human fibroblasts was set up. As substrate, highly radioactive (1.28 Ci/mmol) ganglioside GD1a isotopically tritium-labeled at carbon C-3 of the long chain base was employed; the liberated, and TLC separated [3H]GM1 was determined by computer-assisted radiochromatoscanning. Under experimental conditions that provided a low and quite acceptable (4-5%) coefficient of variation, the detection limit of the method was 0.1 nmol of liberated GM1, using as low as 10 μg of fibroblast homogenate as protein. The detection limit could be lowered to 0.02-0.03 nmol, adopting conditions that, however, carried a higher analytical error (coefficient of variation over 10%). The content of ganglioside sialidase in human fibroblasts cultured in 75-cm2 plastic flasks was 5.8 ∓ 2.5 (SD) nmol liberated GM1 h-1 mg protein-1. Subfractionation studies performed on fibroblast homogenate showed that the ganglioside sialidase was mainly associated ...
Analysis of the Ovine NEU1 Gene in a Unique Model of GM1 Gangliosidosi by Alex Quackenbush"Analysis of the Ovine NEU1 Gene in a Unique Model of GM1 Gangliosidosi" by Alex Quackenbush
Lysosomal Storage Disorders are a class of inherited metabolic conditions that result from alterations in the function of lysosomal enzymes. One example is GM1 Gangliosidosis (GM1), a disorder in which the activity of β-galactosidase is deficient resulting in neurodegeneration and early death. The enzyme, β-gal, is a member of the Lysosomal Multienzyme Complex (LMC), which transports proteins to the lysosome and enables various functions. LMC members include β-gal, α-neuraminidase and the Protective Protein Cathepsin A (PPCA). In a unique ovine model of GM1, there is a primary deficiency in the activity of β- galactosidase and a secondary deficiency in α-neuraminidase activity. The cause of the secondary deficiency in α-neuraminidase activity, which is not seen in any other animal model of GM1, is currently unknown. The α-neuraminidase protein is coded for by the NEU1 gene and is, a glycohydrolitic enzyme that is active in the lysosome. The secondary deficiency of α- neuraminidase seen in our
Influenza Virus Inactivation for Studies of Antigenicity and Phenotypic Neuraminidase Inhibitor Resistance Profiling | Journal...Influenza Virus Inactivation for Studies of Antigenicity and Phenotypic Neuraminidase Inhibitor Resistance Profiling | Journal...
Our study provides validated virus inactivation protocols that allow implementation of phenotypic NAI susceptibility testing, HI assessment (for serology as well antigenic characterization of viruses), and T-cell response characterization using avian, swine, and human influenza viruses under BSL-2 containment conditions. Using pandemic influenza A(H1N1)v virus strains, we illustrate the ease of carrying out Triton X-100 and formalin virus inactivation protocols prior to the assessment of A(H1N1)v virus susceptibility to antivirals and the characterization of B- and T-cell responses, respectively, outside the BSL-3 high-containment facility. These inactivation protocols facilitate the diagnostic examination of pandemic influenza viruses by applying standard laboratory conditions at BSL-2.. Considering results from documented studies and taking ease of use under BSL-3 conditions into account, therefore excluding, e.g., irradiation protocols, we evaluated human A(H3N2) and avian A(H7N3) virus ...
Role of plasma-membrane-bound sialidase NEU3 in clathrin-mediated endocytosis | Biochemical Journal | Portland PressRole of plasma-membrane-bound sialidase NEU3 in clathrin-mediated endocytosis | Biochemical Journal | Portland Press
Gangliosides are sialic acid-containing glycosphingolipids mainly expressed at the outer leaflet of the plasma membrane. Sialidase NEU3 is a key enzyme in the catabolism of gangliosides with its up-regulation having been observed in human cancer cells. In the case of CME (clathrin-mediated endocytosis), although this has been widely studied, the role of NEU3 and gangliosides in this cellular process has not yet been established. In the present study, we found an increased internalization of Tf (transferrin), the archetypical cargo for CME, in cells expressing complex gangliosides with high levels of sialylation. The ectopic expression of NEU3 led to a drastic decrease in Tf endocytosis, suggesting the participation of gangliosides in this process. However, the reduction in Tf endocytosis caused by NEU3 was still observed in glycosphingolipid-depleted cells, indicating that NEU3 could operate in a way that is independent of its action on gangliosides. Additionally, internalization of ...
Neuraminidase and contractile responses to norepinephrine in rat tail artery<...Neuraminidase and contractile responses to norepinephrine in rat tail artery<...
TY - JOUR. T1 - Neuraminidase and contractile responses to norepinephrine in rat tail artery. AU - Rice, J. H.. AU - Webb, R. C.. PY - 1984/1/1. Y1 - 1984/1/1. N2 - Sialic acids are negatively charged groups in the carbohydrate side chains of glycolipids and glycoproteins which line the external membrane surface. The goal of this study was to characterize the effect of neuraminidase, which selectively cleaves sialic acids, on contractile activity in vascular smooth muscle. Helically cut strips of rat tail artery were mounted in an organ chamber and isometric contractions were recorded. Following treatment with neuraminidase (0.2 U/ml, 1 h), contractile responses to norepinephrine were signficantly greater than control responses. Phasic concentrations to norepinephrine in calcium-free medium were not altered by neuraminidase, whereas following calcium depletion with EGTA, contractile responses to added calcium were greater in enzyme-treated strips than in control when activated with ...
Results: Of these 65 patients, 30 received cisplatin plus etoposi | alk-inhibitorsResults: Of these 65 patients, 30 received cisplatin plus etoposi | alk-inhibitors
Background: Little is known about whether neuraminidase inhibitors are effective Vorinostat purchase for children infected with oseltamivir-resistant influenza A(H1N1) viruses.. Methods: Children aged 15 years and younger having influenza-like illness and who visited outpatient clinics within 48 hours Bcl 2 inhibitor of fever onset were enrolled from 2006-2007 to 2008-2009 influenza seasons in Japan. Patients received oseltamivir, zanamivir, or no treatment after screening by a rapid antigen test. Nasopharyngeal swabs were collected before antiviral therapy. and were used for virus isolation. Oseltamivir resistance was determined by detection of the H275Y mutation in neuraminidase, and susceptibility test using neuraminidase inhibition assay. Daily body temperature was evaluated according to drug type and susceptibility by univariate and multivariate analyses.. Results: Of 1647 patients screened, 238 oseltamivir-resistant H1N1 cases (87 oseltamivir-treated, 64 zanamivir-treated, and 87 ...
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Although oseltamivir-resistant pandemic influenza A(H1N1)pdm09 is uncommon in immunocompetent individuals, a recent report from Newcastle, Australia, showed the first sustained community spread, from June to August 2011, of oseltamivir-resistant influenza A(H1N1)pdm09 virus carrying the H275Y neuraminidase (NA) mutation. To determine the frequency and the extent of this viral variant spread in the nearest major city to Newcastle, we performed a sequence-based genotypic assessment on samples from 143 oseltamivir untreated and 23 oseltamivir post-treatment individuals with influenza collected contemporaneously in Sydney, 120 km southwest of Newcastle. The detection of two of 143 (1.4%) community-derived samples containing H275Y suggests a low prevalence of oseltamivir-resistant influenza A(H1N1)pdm09 virus in the general community and no convincing evidence of spread of the NA H275Y-bearing influenza A(H1N1)pdm09 virus. In oseltamivir treated patients, oseltamivir-resistant influenza A(H1N1)pdm09 virus
Construction and comparison of different source neuraminidase candidate vaccine strains for human infection with Eurasian avian...Construction and comparison of different source neuraminidase candidate vaccine strains for human infection with Eurasian avian...
Human infections with Eurasian avian-like swine influenza H1N1 viruses have been reported in China in past years. One case resulted in death and others were mild case. In 2016, the World Health Organization recommended the use of A/Hunan/42443/2015(H1N1) virus to construct the first candidate vaccine strain for Eurasian avian-like swine influenza H1N1 viruses. Previous reports showed that the neuraminidase of A/Puerto Rico/8/34(H1N1) might improve the viral yield of reassortant viruses. Therefore, we constructed two reassortant candidate vaccine viruses of A/Hunan/42443/2015(H1N1) by reverse genetic technology, with (6+2) and (7+1) gene constitution, respectively. The (6+2) virus had hemagglutinin and neuraminidase from A/Hunan/42443/2015, and the (7+1) one had hemagglutinin from A/Hunan/42443/2015, while all the other genes were from A/Puerto Rico/8/34. Our data revealed that although the neuraminidase of the (7+1) virus was from high yield A/Puerto Rico/8/34, the hemagglutination titer and the ...
Cloning and expression of the Bacteroides fragilis TAL2480 neuraminidase gene, nanH, in Escherichia coli. | Journal of...Cloning and expression of the Bacteroides fragilis TAL2480 neuraminidase gene, nanH, in Escherichia coli. | Journal of...
We have cloned the Bacteroides fragilis TAL2480 neuraminidase (NANase) structural gene, nanH, in Escherichia coli. This was accomplished by using the cloning shuttle vector pJST61 and a partial Sau3A library of TAL2480 chromosomal inserts created in E. coli. The library was mobilized into the NANase-deficient B. fragilis TM4000 derivative TC2. NANase-producing colonies were enriched by taking advantage of the inability of TC2, but not the wild-type of NANase+ revertant, to grow in vitro in fluid aspirated from the rat granuloma pouch. Plasmids pJST61-TCN1 and pJST61-TCN3, containing inserts of 9.1 and 4.5 kilobases (kb), respectively, were found in the TC2 derivatives that grew in the rat pouch medium. In B. fragilis, NANase production from the two plasmids was inducible by free N-acetylneuraminic acid or sialic acid-containing substrates, just as in the parental TAL2480 strain. However, when these plasmids were transferred back to E. coli, NANase activity was barely detectable. A 3.5-kb portion ...
Sialic acid catabolism drives intestinal inflammation and microbial dysbiosis in mice - Zurich Open Repository and ArchiveSialic acid catabolism drives intestinal inflammation and microbial dysbiosis in mice - Zurich Open Repository and Archive
Rapid shifts in microbial composition frequently occur during intestinal inflammation, but the mechanisms underlying such changes remain elusive. Here we demonstrate that an increased caecal sialidase activity is critical in conferring a growth advantage for some bacteria including Escherichia coli (E. coli) during intestinal inflammation in mice. This sialidase activity originates among others from Bacteroides vulgatus, whose intestinal levels expand after dextran sulphate sodium administration. Increased sialidase activity mediates the release of sialic acid from intestinal tissue, which promotes the outgrowth of E. coli during inflammation. The outburst of E. coli likely exacerbates the inflammatory response by stimulating the production of pro-inflammatory cytokines by intestinal dendritic cells. Oral administration of a sialidase inhibitor and low levels of intestinal α2,3-linked sialic acid decrease E. coli outgrowth and the severity of colitis in mice. Regulation of sialic acid ...
Study to Assess Efficacy and Safety of Baloxavir Marboxil In Combination With Standard-of-Care Neuraminidase Inhibitor In...Study to Assess Efficacy and Safety of Baloxavir Marboxil In Combination With Standard-of-Care Neuraminidase Inhibitor In...
Clinical trial for Influenza Vaccine | Influenza , Study to Assess Efficacy and Safety of Baloxavir Marboxil In Combination With Standard-of-Care Neuraminidase Inhibitor In Hospitalized Participants With Severe Influenza
Department of Veterinary Public Health and Pharmacology-FVMASDepartment of Veterinary Public Health and Pharmacology-FVMAS
HMTK KARUNARATHNA, RAPM PERERA, VJ FANG, HL YEN, BJ COWLING AND JSM PEIRIS (2016). Serum anti-neuraminidase antibody (Anti-NA N1) responses in human pandemic H1N1 2009 Influenza A virus infections and cross reactivity with seasonal H1N1 virus. Presented at Options IX for the control of influenza conference, Chicago, Illinois, USA held from 24th to 28th August 2016. (Best poster presentation at the symposium in the theme of Public Health ...
Plant Pathology Graduate Program: Rong HaiPlant Pathology Graduate Program: Rong Hai
1. Riegger D*, Hai R*, Dornfeld D, Manz B, Leyva-Grado V, Sanchez-Aparicio MT, Albrecht RA, Palese P, Haller O, Schwemmle M, Garcia-Sastre A, Kochs G, Schmolke M. 2015. The nucleoprotein of newly emerged H7N9 influenza A virus harbors a unique motif conferring resistance to antiviral human MxA. J Virol 89:2241-2252. (*: These authors contributed equally to this work.). 2. Leyva-Grado, V. H.*, Hai, R.*, Fernandes, F., Belicha-Villanueva, A., Carter, C., and Yondola, M. 2014. Modulation of an ectodomain motif in the influenza A virus neuraminidase alters tetherin sensitivity and results in virus attenuation in vivo. Journal of molecular biology 426:1308-1321. (*: These authors contributed equally to this work.). 3. Hai, R., Schmolke, M., Leyva-Grado, V. H., Thangavel, R. R., Margine, I., Jaffe, E. L., Krammer, F., Solorzano, A., Garcia-Sastre, A., Palese, P., and Bouvier, N. M. 2013. Influenza A(H7N9) virus gains neuraminidase inhibitor resistance without loss of in vivo virulence or ...
The release of N-acetyl- and N-glycolloyl-neuraminic acid from soluble complex carbohydrates and erythrocytes by bacterial,...The release of N-acetyl- and N-glycolloyl-neuraminic acid from soluble complex carbohydrates and erythrocytes by bacterial,...
A series of substrates, sialyl(2 leads to 6)GalNAc and ganglioside GM3, containing either N-acetylneuraminic acid (AcNeu) or N-glycolloylneuraminic acid (GcNeu), has been prepared. The trisaccharide GcNeu(2 leads to 3)lactose was preapred by ozonolysis of GcNeu-GM3, and the disaccharides AcNeu(2 leads to 6)GalNAc and GcNeu(2 leads to 6)GalNAc were isolated from bovine submandibular-gland mucin by alkali elimination. Sialidases from Newcastle-disease virus, fowl-plague virus, influenza virus A2, Clostridium perfringens, Vibrio cholerae, Arthrobacter ureafaciens and human liver lysosomes were studied with the above substrates and all showed poorer cleavage of GcNeu-containing substrates when compared with the corresponding AcNeu-containing compounds. This was reflected in the Km and Vmax. values of these sialidases. Differences between viral and bacterial sialidases could be detected on the basis of their kinetic constants and time curves of sialic acid release. Preferred release of AcNeu relative ...
Cancer Translational Science Laboratory | Scientific Computing Research UnitCancer Translational Science Laboratory | Scientific Computing Research Unit
Bacteria are developing resistance against β-lactam antibiotics by various genetic mechanisms of which plasmid acquiring is the most deadly. Amongst others bacteria acquire resistance by degradation or modification of the antibiotic before it reaches the target site, alteration of the antibiotic site and the prevention of access of the antibiotic to the target by forced efflux.. One of the most problematic bacteria known to roam the corridors and wards in hospitals is Staphylococcus aureus, a Gram positive bacterium. We conduct computational structural biology and reaction dynamics studies on S. Aureus to develop lead drugs that may be a new form of antibiotic.. Ian L. Rogers and Kevin J. Naidoo/ Profiling Transition-State Configurations on the Trypanosoma cruzi trans-Sialidase Free-Energy Reaction Surfaces. J. Phys Chem B. 2015. 119, 1192-1201.. Umraan Hendricks, Werner Crous and Kevin J. Naidoo. Computational Rationale for the Selective Inhibition of the Herpes Simplex Virus Type 1 Uracil-DNA ...
Cancer Translational Science Laboratory | Scientific Computing Research UnitCancer Translational Science Laboratory | Scientific Computing Research Unit
Bacteria are developing resistance against β-lactam antibiotics by various genetic mechanisms of which plasmid acquiring is the most deadly. Amongst others bacteria acquire resistance by degradation or modification of the antibiotic before it reaches the target site, alteration of the antibiotic site and the prevention of access of the antibiotic to the target by forced efflux.. One of the most problematic bacteria known to roam the corridors and wards in hospitals is Staphylococcus aureus, a Gram positive bacterium. We conduct computational structural biology and reaction dynamics studies on S. Aureus to develop lead drugs that may be a new form of antibiotic.. Ian L. Rogers and Kevin J. Naidoo/ Profiling Transition-State Configurations on the Trypanosoma cruzi trans-Sialidase Free-Energy Reaction Surfaces. J. Phys Chem B. 2015. 119, 1192-1201.. Umraan Hendricks, Werner Crous and Kevin J. Naidoo. Computational Rationale for the Selective Inhibition of the Herpes Simplex Virus Type 1 Uracil-DNA ...
SWISS-MODEL Template Library | 1s0j.1SWISS-MODEL Template Library | 1s0j.1
SWISS-MODEL Template Library (SMTL) entry for 1s0j.1. Trypanosoma cruzi trans-sialidase in complex with MuNANA (Michaelis complex)
Is Oseltamivir Phosphate Safe - GentaurIs Oseltamivir Phosphate Safe - Gentaur
Description: Oseltamivir is an inhibitor of influenza neuraminidase [1].Oseltamivir is a prodrug that is converted by intestinal and/or hepatic esterases to the neuraminidase inhibitor molecule, oseltamivir carboxylate ...
IJMS | Free Full-Text | Combining Molecular Docking and Molecular Dynamics to Predict the Binding Modes of Flavonoid...IJMS | Free Full-Text | Combining Molecular Docking and Molecular Dynamics to Predict the Binding Modes of Flavonoid...
Control of flavonoid derivatives inhibitors release through the inhibition of neuraminidase has been identified as a potential target for the treatment of H1N1 influenza disease. We have employed molecular dynamics simulation techniques to optimize the 2009 H1N1 influenza neuraminidase X-ray crystal structure. Molecular docking of the compounds revealed the possible binding mode. Our molecular dynamics simulations combined with the solvated interaction energies technique was applied to predict the docking models of the inhibitors in the binding pocket of the H1N1 influenza neuraminidase. In the simulations, the correlation of the predicted and experimental binding free energies of all 20 flavonoid derivatives inhibitors is satisfactory, as indicated by R2 = 0.75.
Identification of amino acid residues at the active site of endosialidase that dissociate the polysialic acid binding and...Identification of amino acid residues at the active site of endosialidase that dissociate the polysialic acid binding and...
Endosialidase (endo-N-acetylneuraminidase) is a tailspike enzyme of bacteriophages specific for human pathogenic Escherichia coli K1, which specifically recognizes and degrades polySia (polysialic acid). polySia is also a polysaccharide of the capsules of other meningitis- and sepsis-causing bacteria, and a post-translational modification of the NCAM (neural cell-adhesion molecule). We have cloned and sequenced three spontaneously mutated endosialidases of the PK1A bacteriophage and one of the PK1E bacteriophage which display lost or residual enzyme activity but retain the binding activity to polySia. Single to triple amino acid substitutions were identified, and back-mutation constructs indicated that single substitutions accounted for only partial reduction of enzymic activity. A homology-based structural model of endosialidase revealed that all substituted amino acid residues localize to the active site of the enzyme. The results reveal the importance of non-catalytic amino acid residues for ...
Potentiation of epidermal growth factor-mediated oncogenic transformation by sialidase NEU3 leading to Src activation. | Sigma...Potentiation of epidermal growth factor-mediated oncogenic transformation by sialidase NEU3 leading to Src activation. | Sigma...
Sigma-Aldrich offers abstracts and full-text articles by [Koji Yamamoto, Kohta Takahashi, Kazuhiro Shiozaki, Kazunori Yamaguchi, Setsuko Moriya, Masahiro Hosono, Hiroshi Shima, Taeko Miyagi].
When flu viruses attack! (video) | Influenza | Khan AcademyWhen flu viruses attack! (video) | Influenza | Khan Academy
Learn how flu viruses get into and out of your cells using Hemagglutinin and Neuraminidase proteins on their surface. Rishi is a pediatric infectious disease physician and works at Khan Academy. These videos do not provide medical advice and are for informational purposes only. The videos are not intended to be a substitute for professional medical advice, diagnosis or treatment. Always seek the advice of a qualified health provider with any questions you may have regarding a medical condition. Never disregard professional medical advice or delay in seeking it because of something you have read or seen in any Khan Academy video.
Role of Transmembrane Domain and Cytoplasmic Tail Amino Acid Sequences of Influenza A Virus Neuraminidase in Raft Association...Role of Transmembrane Domain and Cytoplasmic Tail Amino Acid Sequences of Influenza A Virus Neuraminidase in Raft Association...
The amino acid sequences of the CT and TMD of NA are highly and moderately conserved, respectively, among the influenza A viruses. Yet the specific function and role of these amino acid sequences in virus biology remain unknown. Results presented in this report show that the specific amino acid residues are not absolutely required for the influenza virus life cycle, since either the complete or part of the NA TMD or CT can be replaced and modified, yet infectious viruses can be rescued and propagated. On the other hand, our data show that specific amino acids in some regions of the TMD and CT as well as a foreign TMD have a profound influence on virus biology, causing reduction in growth during multiple cycles of infection. Reduced yield of NA mutants can be attributed to decreased enzyme activity in the virion and a defect in budding at the cell surface.. Mutations in the TMD and CT of NA can affect protein expression, maturation, transport, incorporation into virions, and enzyme activity and ...
Neuraminidase/NA cDNA ORF Clone, Influenza B, N-His tag | SinoBiologicalNeuraminidase/NA cDNA ORF Clone, Influenza B, N-His tag | SinoBiological
With enhanced promotor, Neuraminidase/NA cDNA ORF Clone, Influenza B in pCMV3-SP-N-His is expression-ready, and confirmed by full-length sequence & expression validation
Caltech Biologists Provide Molecular Explanation for the Evolution of Tamiflu Resistance - Healthcanal.com : Healthcanal.comCaltech Biologists Provide Molecular Explanation for the Evolution of Tamiflu Resistance - Healthcanal.com : Healthcanal.com
The study-led by David Baltimore, Caltechs Robert Andrews Millikan Professor of Biology and recipient of the 1975 Nobel Prize in Physiology or Medicine, and postdoctoral scholar Jesse D. Bloom-appears in the June 4 issue of the journal Science. Tamiflu and other antiviral drugs directly target viruses, unlike vaccines, which instead stimulate our bodys immune system to respond to the pathogens after an infection is established. In a flu infection, viruses bind to sialic acid on the surface of a host cell using a protein called hemagglutinin (the "H" in H1N1). The viruses then enter the cell and replicate. When the newly minted viruses exit the cell, they too bind to sialic acid. The viruses then use a protein called neuraminidase (the "N" in H1N1) to cut the sialic acid, freeing themselves to infect new cells. This process, however, is blocked by Tamiflu, which prevents neuraminidase from cleaving the sialic acid. "It does this by binding in the active site of the neuraminidase molecule, ...
Buy cheap Coronavirus (COVID) drug medications onlineBuy cheap Coronavirus (COVID) drug medications online
Coronavirus drug is an antiviral agent that you can buy right now. When taken orally, it is hydrolyzed, turning into an active form of medicine - oseltamivir carboxylate. Its mechanism of action is related to the ability to inhibit neuraminidase (enzymes involved in replication) of influenza viruses A and B. Meanwhile, the ability of viral particles to penetrate the human cells, as well as the exit of virions from an infected human cell, is impaired. This limits the spread of the pathogen through the respiratory tract ...
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Isoenzymes of human liver α-L-fucosidase: Chemical relationship, kinetic studies, and immunochemical characterization |...Isoenzymes of human liver α-L-fucosidase: Chemical relationship, kinetic studies, and immunochemical characterization |...
The chemical relationship of the seven forms of human liver α-L fucosidase has been studied by isoelectric focusing of neuraminidase- and sialyltransf
CATH Domain 2ya5B01CATH Domain 2ya5B01
Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates ...
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A group of 23 volunteers were each inoculated with 600 CCA of a new form of influenza virus A/England/42/72 vaccine; this vaccine consisted of purified haemagglutinin and neuraminidase antigens adsorbed to alhydrogel. No significant reactions to the vaccine were reported. Twenty-two volunteers produced increased titres of serum HI antibody, and all showed increased titres of NI antibody after immunization. Thus, for volunteers with no pre-immunization serum HI antibody, the geometric mean titre of serum antibody increased from 1/5 to 1/196 after immunization. Ten volunteers developed local neutralizing antibody after immunization; this antibody response was detected most frequently in volunteers who showed the greater serum antibody response to immunization, and in nasal washings with the higher concentrations of protein and IgA. Ten weeks after immunization, the vaccinees and a group of matched controls were inoculated intranasally with attenuated A/England/42/72 virus. Evidence of infection ...
This Week in JAMA | JAMA | JAMA NetworkThis Week in JAMA | JAMA | JAMA Network
Widespread use of antiviral therapy can lead to drug resistance, and resistance to neuraminidase inhibitors has been documented in type A influenza. During an i
Proteasom - WikipediaProteasom - Wikipedia
Proteazomi su proteinski kompleksi koji su nađeni svih eukariota i Archaea, a i kod nekih bakterija. Kod eukariota se nalaze u jedru i citoplazmi.[1] Glavna funkcija proteazoma je razgradnja nepotrebnih ili oštećenih proteina, u procesu proteolize, odnosno hemijske reakcije u kojoj se razlažu peptidne veze. Enzimi koji kataliziraju ove reakcije su proteaze.[2][3][4] Proteazomi su dio velikog mehanizma kojim ćelije reguliraju koncentraciju pojedinih proteina i razgrađuju nepravilno savijene proteine. U procesu degradacije nastaju peptidi sa oko sedam do osam aminokiselina, koji se zatim razrađuju u aminokiseline i koriste u sintezi novih proteina.[5] Za degradaciju, proteini se obilježavaju malim proteinom zvanim ubikvitin. Reakcija obilježavanja se katalizira enzimima ubikvitinskim ligazama. Vezanje jednog ubikvitina na protein je signal drugim ligazama da vežu dodatne molekule ubikvitina. Rezultat je poliubikvitinski lanac za koji se veže proteazom, što omogućava degradaciju ...
GLB1GLB1
Alfred Gottschalk (biochemist)Alfred Gottschalk (biochemist)
Cathepsin ACathepsin A
NEU1NEU1
InfluenzaInfluenza
ZanamivirZanamivir
Micromonospora viridifaciensMicromonospora viridifaciens
George C. RoyalGeorge C. Royal
Glycoside hydrolase family 34Glycoside hydrolase family 34
LaninamivirLaninamivir
Peter ColmanPeter Colman
Kelch motifKelch motif
Streptomyces seoulensisStreptomyces seoulensis
Influenza treatmentInfluenza treatment
Amurensin KAmurensin K
InfluenzaInfluenza
Hypholomine BHypholomine B
OseltamivirOseltamivir
PeramivirPeramivir
Rubella virusRubella virus
Influenza A virus subtype H5N1Influenza A virus subtype H5N1
Oseltamivir total synthesisOseltamivir total synthesis
Influenza A virus subtype H5N1Influenza A virus subtype H5N1
OrthomyxoviridaeOrthomyxoviridae
Influenza A virus subtype H1N1Influenza A virus subtype H1N1
ParamyxoviridaeParamyxoviridae
Stockpiling antiviral medications for pandemic influenzaStockpiling antiviral medications for pandemic influenza
GalactosialidosisGalactosialidosis
Community-acquired pneumoniaCommunity-acquired pneumonia
AnatomyOrganismsDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesInformation ScienceHealth Care
NeuraminidaseZanamivirSialic AcidsOseltamivirInfluenza A virusPyransNeuraminic AcidsOrthomyxoviridaeN-Acetylneuraminic AcidHemagglutinin Glycoproteins, Influenza VirusInfluenza, HumanHemagglutination, ViralGuanidinesAntiviral AgentsInfluenza A Virus, H1N1 SubtypeHemagglutinins, ViralOrthomyxoviridae InfectionsInfluenza B virusInfluenza A Virus, H3N2 SubtypeInfluenza A Virus, H5N1 SubtypeInfluenza in BirdsDrug Resistance, ViralGalactose OxidaseFerretsHemagglutination Inhibition TestsHemagglutininsHN ProteinReassortant VirusesLectinsAcetamidesInfluenza A Virus, H2N2 SubtypeInfluenza A Virus, H7N9 SubtypeInfluenza A Virus, H9N2 SubtypeDogsNewcastle disease virusInfluenza VaccinesClostridium perfringensViral ProteinsCell LineGlycoproteinsWheat Germ AgglutininsParainfluenza Virus 3, HumanMadin Darby Canine Kidney CellsCarbohydratesHemadsorptionPeanut AgglutininDucksBirdsCathepsin AReceptors, VirusGangliosidesViral Plaque AssayCyclopentanesGlycosylationHemagglutination TestsParamyxoviridaeMolecular Sequence DataHymecromoneErythrocytesPeriodic AcidGlycoside HydrolasesEnzyme InhibitorsMucolipidosesMolecular WeightHemagglutinationAntibodies, ViralArthrobacterPandemicsAmantadineChick EmbryoVirus ReplicationSialoglycoproteinsPronaseElectrophoresis, Polyacrylamide GelTrypsinPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidaseActinomycetaceaeCell MembraneChickensParainfluenza Virus 1, HumanIsoelectric FocusingRespirovirusAmino Acid SequenceMutationEpitopesMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseOxo-Acid-Lyases
Anti-Swine H1N1 Neuraminidase antibody (ab91643) ProtocolsAnti-Swine H1N1 Neuraminidase antibody (ab91643) Protocols
Cutting through mucus with the influenza virus neuraminidaseCutting through mucus with the influenza virus neuraminidase
Autoimmune Reactions Against Liver Cells by Syngeneic Neuraminidase-Treated Lymphocytes | The Journal of ImmunologyAutoimmune Reactions Against Liver Cells by Syngeneic Neuraminidase-Treated Lymphocytes | The Journal of Immunology
British Library EThOS: Structure and function of a neuraminidase from Streptococcus pneumoniaeBritish Library EThOS: Structure and function of a neuraminidase from Streptococcus pneumoniae
Neuraminidase - BP941 | acris-antibodies.comNeuraminidase - BP941 | acris-antibodies.com
Inhibition of Neuraminidase Inhibitor-Resistant Influenza Virus by DAS181, a Novel Sialidase Fusion ProteinInhibition of Neuraminidase Inhibitor-Resistant Influenza Virus by DAS181, a Novel Sialidase Fusion Protein
Neuraminidase (Isoenzyme S), 1U - EY Laboratories, Inc.Neuraminidase (Isoenzyme S), 1U - EY Laboratories, Inc.
Anti-Influenza B Virus Neuraminidase Antibody | Mouse Monoclonal | LSBioAnti-Influenza B Virus Neuraminidase Antibody | Mouse Monoclonal | LSBio
Neuraminidase is important for the initiation of influenza virus infection in human airway epitheliumNeuraminidase is important for the initiation of influenza virus infection in human airway epithelium
Recombinant H7N9 Neuraminidase/NA Protein, HEK293 Cells, 40108-VNAHC | Sino BiologicalRecombinant H7N9 Neuraminidase/NA Protein, HEK293 Cells, 40108-VNAHC | Sino Biological
Neuraminidase - WikipediaNeuraminidase - Wikipedia
Hemagglutinin-neuraminidase - WikipediaHemagglutinin-neuraminidase - Wikipedia
neuraminidase - Everything2.comneuraminidase - Everything2.com
Neuraminidase - definition of neuraminidase by The Free DictionaryNeuraminidase - definition of neuraminidase by The Free Dictionary
Neuraminidase Inhibitors Improve Survival in Kids With FluNeuraminidase Inhibitors Improve Survival in Kids With Flu
Neuraminidase Inhibitors for Critically Ill Children With Influenza | Articles | PediatricsNeuraminidase Inhibitors for Critically Ill Children With Influenza | Articles | Pediatrics
Eurosurveillance | Introduction of neuraminidase inhibitor zanamivirEurosurveillance | Introduction of neuraminidase inhibitor zanamivir
α2-3,6,8 Neuraminidase | NEBα2-3,6,8 Neuraminidase | NEB
Influenza neuraminidase inhibitors: antiviral action and mechanisms of resistance. - PubMed - NCBIInfluenza neuraminidase inhibitors: antiviral action and mechanisms of resistance. - PubMed - NCBI
RCSB PDB - Protein Feature View - Neuraminidase - P03474 (NRAM INBLE)RCSB PDB - Protein Feature View - Neuraminidase - P03474 (NRAM INBLE)
Gangliosides, Neuraminidase and Sialyltransferase at the Nerve Endings | SpringerLinkGangliosides, Neuraminidase and Sialyltransferase at the Nerve Endings | SpringerLink
The neuraminidase of influenza virusThe neuraminidase of influenza virus
RCSB PDB - 6EKS: Vibrio cholerae neuraminidase complexed with oseltamivir carboxylateRCSB PDB - 6EKS: Vibrio cholerae neuraminidase complexed with oseltamivir carboxylate
Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III. - PubMed - NCBIStructure of the haemagglutinin-neuraminidase from human parainfluenza virus type III. - PubMed - NCBI
PRIME PubMed | Two neuraminidase inhibitors for treatment of influenzaPRIME PubMed | Two neuraminidase inhibitors for treatment of influenza
Positive Regulation of Insulin Signaling by Neuraminidase 1 | DiabetesPositive Regulation of Insulin Signaling by Neuraminidase 1 | Diabetes
Neuraminidase - GanfydNeuraminidase - Ganfyd
Neuraminidase - Proteopedia, life in 3DNeuraminidase - Proteopedia, life in 3D
The neuraminidase of influenza virusThe neuraminidase of influenza virus
Eurosurveillance | Benefit of oral neuraminidase inhibitor oseltamivir in natural influenzaEurosurveillance | Benefit of oral neuraminidase inhibitor oseltamivir in natural influenza
Biological evaluation of Radix Isatidis based on neuraminidaseBiological evaluation of Radix Isatidis based on neuraminidase
Anti-Influenza A Neuraminidase 1 antibody (ab119972) | AbcamAnti-Influenza A Neuraminidase 1 antibody (ab119972) | Abcam
Molecules | Free Full-Text | Influenza Neuraminidase Inhibitors: Synthetic Approaches, Derivatives and Biological ActivityMolecules | Free Full-Text | Influenza Neuraminidase Inhibitors: Synthetic Approaches, Derivatives and Biological Activity
Universal anti-neuraminidase antibody inhibiting all influenza A subtypesUniversal anti-neuraminidase antibody inhibiting all influenza A subtypes
Seasonal H1N1 Neuraminidase Research Products: Novus BiologicalsSeasonal H1N1 Neuraminidase Research Products: Novus Biologicals
HN - Hemagglutinin-neuraminidase - Parainfluenza virus 5 (strain W3) (PIV5) - HN gene & proteinHN - Hemagglutinin-neuraminidase - Parainfluenza virus 5 (strain W3) (PIV5) - HN gene & protein
NEU1 - Neuraminidase 1 - Gorilla gorilla gorilla (Western lowland gorilla) - NEU1 gene & proteinNEU1 - Neuraminidase 1 - Gorilla gorilla gorilla (Western lowland gorilla) - NEU1 gene & protein
Frontiers | Neuraminidase-3 Is a Negative Regulator of LFA-1 Adhesion | ChemistryFrontiers | Neuraminidase-3 Is a Negative Regulator of LFA-1 Adhesion | Chemistry
AnatomyOrganismsDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesInformation ScienceHealth Care
NeuraminidaseZanamivirSialic AcidsOseltamivirInfluenza A virusPyransNeuraminic AcidsOrthomyxoviridaeN-Acetylneuraminic AcidHemagglutinin Glycoproteins, Influenza VirusInfluenza, HumanHemagglutination, ViralGuanidinesAntiviral AgentsInfluenza A Virus, H1N1 SubtypeHemagglutinins, ViralOrthomyxoviridae InfectionsInfluenza B virusInfluenza A Virus, H3N2 SubtypeInfluenza A Virus, H5N1 SubtypeInfluenza in BirdsDrug Resistance, ViralGalactose OxidaseFerretsHemagglutination Inhibition TestsHemagglutininsHN ProteinReassortant VirusesLectinsAcetamidesInfluenza A Virus, H2N2 SubtypeInfluenza A Virus, H7N9 SubtypeInfluenza A Virus, H9N2 SubtypeDogsNewcastle disease virusInfluenza VaccinesClostridium perfringensViral ProteinsCell LineGlycoproteinsWheat Germ AgglutininsParainfluenza Virus 3, HumanMadin Darby Canine Kidney CellsCarbohydratesHemadsorptionPeanut AgglutininDucksBirdsCathepsin AReceptors, VirusGangliosidesViral Plaque AssayCyclopentanesGlycosylationHemagglutination TestsParamyxoviridaeMolecular Sequence DataHymecromoneErythrocytesPeriodic AcidGlycoside HydrolasesEnzyme InhibitorsMucolipidosesMolecular WeightHemagglutinationAntibodies, ViralArthrobacterPandemicsAmantadineChick EmbryoVirus ReplicationSialoglycoproteinsPronaseElectrophoresis, Polyacrylamide GelTrypsinPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidaseActinomycetaceaeCell MembraneChickensParainfluenza Virus 1, HumanIsoelectric FocusingRespirovirusAmino Acid SequenceMutationEpitopesMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseOxo-Acid-Lyases
InhibitorSialidaseH1N1ProteinProteinsAntibodySubtypesVirusesSialicGlycoproteinsRecombinantGeneBacterial neuraminidasesAvian influZanamivir and oseltamivirEnzyme neuraminidaseGlycoproteinInhibitionWild-type and mutatedLevels of neuraminidase activityType 3 hemagglutinin-neuraminidaseMammalianAntiviralAssayH5N1NAIsPotent neuraminidase inhibitorsDevelopmentally regulated neuraminidaseAntibodiesParainfluenzaTypes of neuraminidaseResistanceEnzymes that cleaveViral neuraminidasesBiologicalStrainsAntigenicStreptococcusSpecific neuraminidaseResiduesSubstrateInfectionActivityNeuraminic acidOseltamivir carboxylateParamyxovirusesEnzymatic
Inhibitor22
Sialidase10
H1N119
Protein21
Proteins10
Antibody5
Subtypes4
Viruses11
Sialic12
  • Neuraminidases, also called sialidases, catalyze the hydrolysis of terminal sialic acid residues from the newly formed virions and from the host cell receptors. (wikipedia.org)
  • Sialic acid 3 is now more often called N-acetyl neuraminic acid , and hence the name of RDE was changed yet again, this time to neuraminidase. (everything2.com)
  • There are two major classes of Neuraminidase that cleave exo or endo poly-sialic acids: Exo hydrolysis of α-(2→3)-, α-(2→6)-, α-(2→8)-glycosidic linkages of terminal sialic acid residues Endo hydrolysis of (2→8)-α-sialosyl linkages in oligo- or poly(sialic) acids Neuraminidases, also called sialidases, catalyze the hydrolysis of terminal sialic acid residues from the newly formed virions and from the host cell receptors. (wikipedia.org)
  • α2-3,6,8 Neuraminidase catalyzes the hydrolysis of α2-3, α2-6, and α2-8 linked sialic acid residues from glycoproteins and oligosaccharides. (neb.com)
  • Parainfluenza virus type 3 hemagglutinin-neuraminidase is expressed by HPIV paramyxoviruses that bind to sialic acid-containing receptor molecules on the surface of host lung cells. (functionalglycomics.org)
  • The current strategy for treating influenza focuses on inhibiting the function of neuraminidase, which is an enveloped enzyme located on the surface of both influenza A and B. Influenza neuraminidase is an exosialidase that recognizes the α -ketosidic linkage between neuraminic acid (or sialic acid) and carbohydrate residues ( Von Itzstein, 2011 ). (peerj.com)
  • The main function of influenza neuraminidase (NA) involves enzymatic cleavage of sialic acid from the surface of host cells resulting in the release of the newly produced virions from infected cells, as well as aiding the movement of virions through sialylated mucus present in the respiratory tract. (hku.hk)
  • Our objectives were then to investigate both sialic acid binding and cleavage of neuraminidase at an atomic resolution level. (hku.hk)
  • Neuraminidase digestion abolished WGA binding to the proximal ciliary membrane surface, indicating that sialic acids mediate WGA binding to this domain. (arvojournals.org)
  • Neuraminidases are enzymes that cleave sialic acid groups from glycoproteins. (sinobiological.com)
  • Neuraminidase, on the other hand, cleaves the HA-sialic acid bondage from the newly formed virions and the host cell receptors during budding. (sinobiological.com)
  • Neuraminidase removes terminal sialic acid residues from glycoproteins. (roche.com)
Glycoproteins5
Recombinant3
Gene11
  • Here, we describe a mutation in IAV nucleoprotein (NP) that enhances replication and transmission in guinea pigs while selectively reducing neuraminidase (NA) gene segment packaging into virions. (pnas.org)
  • The sequence of the cloned neuraminidase gene (nan A), was compared to other bacterial neuraminidases to identify conserved residues, and also utilising crystallography data, predictions were made of the residues likely to be important in catalysis. (bl.uk)
  • Cloning and expression of the Bacteroides fragilis TAL2480 neuraminidase gene, nanH, in Escherichia coli. (asm.org)
  • We have cloned the Bacteroides fragilis TAL2480 neuraminidase (NANase) structural gene, nanH, in Escherichia coli. (asm.org)
  • Here, we assessed the ability of a novel dual-specific anti-tumor oncolytic adenovirus, expressing the hemagglutinin-neuraminidase (HN) gene from the Newcastle disease virus under the human telomerase reverse transcriptase (hTERT) promoter (Ad-hTERTp-E1a-HN), to inhibit esophageal cancer EC-109 cells in culture and to reduce tumor burden in xenografted BALB/c nude mice. (mdpi.com)
  • Streptococcus pneumoniae is believed to produce more than one form of neuraminidase, but there has been uncertainty as to whether this is due to posttranslational modification of a single gene product or the existence of more than one neuraminidase-encoding gene. (asm.org)
  • Only one stable pneumococcal neuraminidase gene (designated nanA) has been described. (asm.org)
  • In the present study, we isolated and characterized a second neuraminidase gene (designated nanB), which is located close to nanA on the pneumococcal chromosome (approximately 4.5kb downstream). (asm.org)
  • A gene from Streptococcus pneumoniae (nanA), with features entirely consistent with a neuraminidase gene, has been sequenced. (asm.org)
  • High levels of neuraminidase activity were obtained after cloning of this gene, without flanking sequences, into a high-expression vector. (asm.org)
  • The nanH structural gene for neuraminidase was cloned from B. fragilis TM4000 and was used to create two isogenic strains with chromosomal disruptions at the nanH gene. (asm.org)
Bacterial neuraminidases2
  • The Trypanosoma cruzi neuraminidase contains sequences similar to bacterial neuraminidases, YWTD repeats of the low density lipoprotein receptor, and type III modules of fibronectin. (rupress.org)
  • NanA contains the four copies of the sequence SXDXGXTW that is present in all the bacterial neuraminidases previously described. (asm.org)
Avian influ1
Zanamivir and oseltamivir1
Enzyme neuraminidase3
Glycoprotein2
Inhibition5
Wild-type and mutated1
Levels of neuraminidase activity1
  • Dynamic range of four orders of magnitude enables you to quantitate virus isolates over a broad range of virus concentration and with varying levels of neuraminidase activity without performing numerous sample dilutions. (thermofisher.com)
Type 3 hemagglutinin-neuraminidase2
Mammalian2
Antiviral2
Assay5
H5N11
NAIs5
Potent neuraminidase inhibitors1
Developmentally regulated neuraminidase1
  • Trypanosoma cruzi expresses a developmentally regulated neuraminidase (TCNA) implicated in parasite invasion of cells. (rupress.org)
Antibodies7
  • Antibodies which inhibit the enzyme limit the infection, but antigenic variation of the neuraminidase renders it ineffective in a vaccine. (nih.gov)
  • Escape mutants, selected by growing virus in the presence of monoclonal antibodies to the neuraminidase, possess single amino acid sequence changes. (nih.gov)
  • We have studied the maturation of the influenza A virus neuraminidase (NA), using monoclonal antibodies (MAbs) with different conformational specificities against the head domains of the N8 NA. (asm.org)
  • The wide range of reactivity probably relates to the infection history of the donor, whose plasmablasts generated antibodies with long regions that insert into the active site of the neuraminidase enzyme. (flutrackers.com)
  • We describe three human monoclonal antibodies isolated from an H3N2-infected donor that bind with exceptional breadth to multiple different influenza A and B virus neuraminidases. (flutrackers.com)
  • These antibodies neutralize the virus, mediate effector functions, are broadly protective in vivo, and inhibit neuraminidase activity by directly binding to the active site. (flutrackers.com)
  • Structural and functional characterization of these antibodies will inform the development of neuraminidase-based universal vaccines against influenza virus. (flutrackers.com)
Parainfluenza4
Types of neuraminidase2
  • Swiss-Prot lists 137 types of neuraminidase from various species as of October 18, 2006. (wikipedia.org)
  • Three types of neuraminidase are found in mammals and are defined as lysosomal, plasma membrane and cytosolic on the basis of their biochemical properties and subcellular distribution. (acris-antibodies.com)
Resistance1
Enzymes that cleave1
Viral neuraminidases1
Biological2
Strains2
Antigenic1
Streptococcus1
  • The protective effects of the mutated neuraminidases in mice was investigated by immunization followed by challenge with virulent Streptococcus penumoniae. (bl.uk)
Specific neuraminidase2
  • The specific neuraminidase activity of infective trypomastigotes obtained from tissue culture and from the bloodstream of infected mice is 7 to 15 times higher than that of the acellular culture forms. (sciencemag.org)
  • This study did not evaluate specific neuraminidase inhibitors. (lasvegasemr.com)
Residues2
  • However, they displayed cumulative mutations in and around the linear epitope of hemagglutinin-neuraminidase (residues 345 to 353) with time. (asm.org)
  • Neuraminidase is an important deglycosylation enzyme capable of cleaving all non-reducing unbranched N-acetylneuraminic and N-glycolylneuraminic acid residues by hydrolysis of α (2→6), α (2→3), α (2→8), and α (2→9) linkages (affinity in the order given). (creative-enzymes.com)
Substrate3
  • Two fold dilutions of α2-3,6,8 Neuraminidase are incubated with 1 nmol AMC-labeled substrate and 1X GlycoBuffer 1 in a 10 µl reaction. (neb.com)
  • S. Herlambang and R. Saleh, "The Comparison of Substrate Stability in Neuraminidase Type 2 (N2) Active Site between A/Tokyo/3/67 and A/Pennsylvania/10218/84 with Heating Dynamics Simulation," World Journal of Condensed Matter Physics , Vol. 1 No. 3, 2011, pp. 77-87. (scirp.org)
  • The PNAS was designed and manufactured to quantitatively identify the levels of neuraminidase in the sample, which is based on colorimetric analysis using the X-Neu5Ac substrate. (koreascience.or.kr)
Infection3
Activity11
  • We have investigated the mechanism and activity of the human neuraminidase (NEU) isoenzyme, NEU3, on T cell adhesion receptors. (frontiersin.org)
  • Successful heat inactivation coincided with the loss of hemagglutinin (HA) and neuraminidase (NA) characteristics, and β-propiolactone inactivation reduced the hemagglutination titer and NA activity of the human influenza virus 10-fold or more. (asm.org)
  • Brain tissue is especially rich in membrane-bound neuraminidase which reaches its highest specific activity in the plasma membranes isolated from synaptosomes (2, 3). (springer.com)
  • The human pathogen Trypanosoma cruzi (Y strain) contains a neuraminidase activity that varies widely in the different developmental stages of the parasite. (sciencemag.org)
  • Neuraminidase shows normal activity even in the presence of 1% BME, and 0.5% SDS. (neb.com)
  • Two Bacteroides fragilis neuraminidase-deficient mutants were used to study the role of neuraminidase activity in growth of B. fragilis in tissue culture monolayers (CHO cells) and in the in vivo rat granuloma pouch. (asm.org)
  • We suggest that neuraminidase activity may be required for B. fragilis to grow to maximal levels in the tissue culture and rat pouch systems by making other carbon sources available after glucose levels are reduced. (asm.org)
  • Meanwhile, SJS targeted on neuraminidase of influenza virus as SJS at 2 mg/ml inhibited 80% of neuraminidase enzymatic activity. (biomedcentral.com)
  • 1,2 These compounds were designed to interfere with the activity of the neuraminidase enzyme of the influenza virus based on knowledge of the three-dimensional crystal structure of the enzyme, determined by Australian scientists, and of the chemistry of its interaction with cell surface receptors. (health.gov.au)
  • Model showed that electrostatic and steric interactions play important role in determining neuraminidase inhibitory activity. (jbsdonline.com)
  • A DNA sequence encoding the Influenza A virus (A/Anhui/1/2013(H7N9)) Neuraminidase (translated amino acids of EPI439509) (His36-Leu465) was expressed , the cell lysates are collected, and bio-activity was tested. (sinobiological.com)
Neuraminic acid1
Oseltamivir carboxylate2
Paramyxoviruses1
Enzymatic1
Inhibition of Neuraminidase Inhibitor-Resistant Influenza Virus by DAS181, a Novel Sialidase Fusion Protein
Inhibition of Neuraminidase Inhibitor-Resistant Influenza Virus by DAS181, a Novel Sialidase Fusion Protein (journals.plos.org)
1ivg - Proteopedia, life in 3D
1ivg - Proteopedia, life in 3D (proteopedia.org)
Cutting through mucus with the influenza virus neuraminidase
Cutting through mucus with the influenza virus neuraminidase (virology.ws)
Neuraminidase - Wikipedia
Neuraminidase - Wikipedia (en.wikipedia.org)
Antiviral Drugs for Seasonal Influenza: Additional Links and Resources | CDC
Antiviral Drugs for Seasonal Influenza: Additional Links and Resources | CDC (cdc.gov)
Alfred Gottschalk | British biochemist | Britannica.com
Alfred Gottschalk | British biochemist | Britannica.com (britannica.com)
A structure-based rationale for sialic acid independent host-cell entry of Sosuga virus | PNAS
A structure-based rationale for sialic acid independent host-cell entry of Sosuga virus | PNAS (pnas.org)
Production and Characterization of Human Monoclonal Antibodies against Gram-Negative Bacteria | SpringerLink
Production and Characterization of Human Monoclonal Antibodies against Gram-Negative Bacteria | SpringerLink (link.springer.com)
Tulane virus recognizes sialic acids as cellular receptors | Scientific Reports
Tulane virus recognizes sialic acids as cellular receptors | Scientific Reports (nature.com)
UCSF ChimeraX Example Images
UCSF ChimeraX Example Images (cgl.ucsf.edu)
Neuraminidase Inhibitors Improve Survival in Kids With Flu
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Influenza - Wikipedia
Influenza - Wikipedia (en.m.wikipedia.org)
Influenza: Optimizing Prevention and Treatment Strategies
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NEU1 gene - Genetics Home Reference - NIH
NEU1 gene - Genetics Home Reference - NIH (ghr.nlm.nih.gov)
Products | NEB
Products | NEB (neb.com)
Gangliosides, Neuraminidase and Sialyltransferase at the Nerve Endings | SpringerLink
Gangliosides, Neuraminidase and Sialyltransferase at the Nerve Endings | SpringerLink (link.springer.com)
CDC - Seasonal Influenza (Flu) - Weekly Report: Influenza Summary Update
CDC - Seasonal Influenza (Flu) - Weekly Report: Influenza Summary Update (cdc.gov)
ILINet State Activity Indicator Map Widget
ILINet State Activity Indicator Map Widget (cdc.gov)
CDC - Seasonal Influenza (Flu) - Weekly Report: Influenza Summary Update
CDC - Seasonal Influenza (Flu) - Weekly Report: Influenza Summary Update (cdc.gov)
(cdc.gov)
CDC - Seasonal Influenza (Flu) - Weekly Report: Influenza Summary Update
CDC - Seasonal Influenza (Flu) - Weekly Report: Influenza Summary Update (cdc.gov)
CDC - Seasonal Influenza (Flu) - Weekly Report: Influenza Summary Update
CDC - Seasonal Influenza (Flu) - Weekly Report: Influenza Summary Update (cdc.gov)
(cdc.gov)