Antigenic determinants of influenza virus haemagglutinin. VI. Antigenic characterization of the oligosaccharide sidechains from HA1of influenza virus haemagglutinins Journal Articles ...
Using the Octet RED system, Kd values for S139/1 Fab and IgG binding to various influenza HA strains were determined to assess enhanced virus neutralization effects due to avidity of full IgG vs. Fab. Biotinylated HA and Streptavidin biosensors were used for these measurements. The increased avidity of IgG binding was shown to reduce Kd values and improve ability of S139/1 to recognize different heterosubtypes of the virus. The Kd data correlated with neutralization data.
In the polarized kidney cell line MDCK, the influenza virus hemagglutinin (HA) has been well characterized as a model for apically sorted membrane glycoproteins. Previous work from our laboratory has shown that a single amino acid change in the cytoplasmic sequence of HA converts it from a protein that is excluded from coated pits to one that is efficiently internalized. Using trypsin or antibodies to mark protein on the surface, we have shown in MDCK cells that HA containing this mutation is no longer transported to the apical surface but instead is delivered directly to the basolateral plasma membrane. We propose that a cytoplasmic feature similar to an endocytosis signal can cause exclusive basolateral delivery. ...
Summary The oligosaccharide sidechains attached to the major polypeptide, HA1 of the haemagglutinin of influenza virus were examined for antigenic activity using a solid-phase radioimmunoassay. Cross-reactivity between the HA1 of different human subtypes was clearly demonstrable with IgG raised against purified virus but was abrogated if anti-carbohydrate antibodies were first removed by passage of the IgG through an immunoadsorbent column containing haemagglutinin (HA) from an unrelated avian influenza strain. Antibodies eluted from the column were found to cross-react with the HA1 of all subtypes tested. Host antigen extracted from chick chorioallantoic membrane and coupled to Sepharose was also able to remove cross-reactive antibodies from antiviral sera, while antibodies raised against host antigen bound to the HA1 isolated from each subtype tested. It is concluded that, although there are qualitative and quantitative differences between the oligosaccharide sidechains of influenza haemagglutinins,
1HGD: BINDING OF INFLUENZA VIRUS HEMAGGLUTININ TO ANALOGS OF ITS CELL-SURFACE RECEPTOR, SIALIC ACID: ANALYSIS BY PROTON NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY AND X-RAY CRYSTALLOGRAPHY
Citation. Das SR, Hensley SE, Ince WL, Brooke CB, Subba A, Delboy MG, Russ G, Gibbs JS, Bennink JR, Yewdell JW. Defining Influenza A Virus Hemagglutinin Antigenic Drift by Sequential Monoclonal Antibody Selection.. Cell Host & Microbe. 2013 Mar 13; 13: 314-23.. External Citation. Abstract. Human influenza A virus (IAV) vaccination is limited by antigenic drift, rapid antibody-driven escape reflecting amino acid substitutions in the globular domain of hemagglutinin (HA), the viral attachment protein. To better understand drift, we used anti-hemagglutinin monoclonal Abs (mAbs) to sequentially select IAV escape mutants. Twelve selection steps, each resulting in a single amino acid substitution in the hemagglutinin globular domain, were required to eliminate antigenicity defined by monoclonal or polyclonal Abs. Sequential mutants grow robustly, showing the structural plasticity of HA, although several hemagglutinin substitutions required an epistatic substitution in the neuraminidase glycoprotein ...
Murine hybridomas producing neutralizing mAbs specific to the pandemic influenza virus A/California/07/2009 haemagglutinin (HA) were isolated. These antibodies recognized at least two different but overlapping new epitopes that were conserved in the HA of most Spanish pandemic isolates. However, one of these isolates (A/Extremadura/RR6530/2010) lacked reactivity with the mAbs and carried two unique mutations in the HA head (S88Y and K136N) that were required simultaneously to eliminate reactivity with the murine antibodies. This unusual requirement directly illustrates the phenomenon of enhanced antigenic change proposed previously for the accumulation of simultaneous amino acid substitutions at antigenic sites of the influenza A virus HA during virus evolution (Shih et al., Proc Natl Acad Sci USA, 104 , 6283-6288, 2007). The changes found in the A/Extremadura/RR6530/2010 HA were not found in escape mutants selected in vitro with one of the mAbs, which contained instead nearby single amino acid changes
2KXA: The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface.
Citation. Magadán JG, Khurana S, Das SR, Frank GM, Stevens J, Golding H, Bennink JR, Yewdell JW. Influenza a Virus Hemagglutinin Trimerization Completes Monomer Folding and Antigenicity.. Journal of Virology. 2013 Sep 01; 87: 9742-53.. External Citation. Abstract. Influenza A virus (IAV) remains an important human pathogen largely because of antigenic drift, the rapid emergence of antibody escape mutants that precludes durable vaccination. The most potent neutralizing antibodies interact with cognate epitopes in the globular head domain of hemagglutinin (HA), a homotrimeric glycoprotein. The H1 HA possesses five distinct regions defined by a large number of mouse monoclonal antibodies (MAbs), i.e., Ca1, Ca2, Cb, Sa, and Sb. Ca1-Ca2 sites require HA trimerization to attain full antigenicity, consistent with their locations on opposite sides of the trimer interface. Here, we show that full antigenicity of Cb and Sa sites also requires HA trimerization, as revealed by immunofluorescence ...
There are no specific protocols for Recombinant Influenza A Virus Hemagglutinin H5 protein (ab69748). Please download our general protocols booklet
Avian-derived influenza A zoonoses are closely monitored and may be a sign of virus strains with pandemic potential. using fluorescent protein with nonoverlapping emission spectra, this book bivalent fluorescence-based microneutralization assay (BiFMA) may be used to detect neutralizing antibodies against two distinctive influenza isolates within a response, doubling the quickness of experimentation while halving the quantity of sera required. Furthermore, this approach could be employed for the speedy id of influenza broadly neutralizing antibodies. Significantly, this book BiFMA could be used for just about any provided influenza HA-pseudotyped trojan under BSL-2 services, including extremely pathogenic influenza HA isolates. trojan rescue. Instead of non-influenza disease pseudotypes, sciIAV maintains appropriate HA:NA stoichiometry, virion morphology, and once sciIAV is usually rescued, the backbone disease can be pseudotyped on varied HA-expressing cells more rapidly than rescuing new ...
Das Hüllglykoprotein Hämagglutinin (HA) von Influenzavirus ist verantwortlich sowohl für die Bindung als auch für die nachfolgende Fusion der viralen Hülle mit der endosomalen Membran. Eine Analyse der 3D Struktur der HA-Ektodomaine zeigt, dass die Stabilität des Proteins sowohl durch kovalente als auch durch nicht-kovalente Wechselwirkungen bedingt ist. Die Konformationsänderung von HA bei saurem pH-Wert weißt auf eine mögliche Rolle von Protonierungseffekten auf ionisierbare Aminosäuren hin. Untersuchungen zur Bedeutung geladener Aminosäuren und Salzbrücken für die Struktur des HA wurden auf der Grundlage von ‚site directed mutagenesis durchgeführt. Der Einfluss der Mutationen auf die Konformationsänderung und die Fusionsaktivität von HA wurden durch einen Proteinase K-Assay bzw. Fluoreszenzmikroskopie erfasst. Die Ergebnisse beider Methoden wurden miteinander korreliert. Abgesehen von der Mutante R109E zeigten Wildtyp-HA und alle anderen Mutanten eine vergleichbare ...
Das Hüllglykoprotein Hämagglutinin (HA) von Influenzavirus ist verantwortlich sowohl für die Bindung als auch für die nachfolgende Fusion der viralen Hülle mit der endosomalen Membran. Eine Analyse der 3D Struktur der HA-Ektodomaine zeigt, dass die Stabilität des Proteins sowohl durch kovalente als auch durch nicht-kovalente Wechselwirkungen bedingt ist. Die Konformationsänderung von HA bei saurem pH-Wert weißt auf eine mögliche Rolle von Protonierungseffekten auf ionisierbare Aminosäuren hin. Untersuchungen zur Bedeutung geladener Aminosäuren und Salzbrücken für die Struktur des HA wurden auf der Grundlage von ‚site directed mutagenesis durchgeführt. Der Einfluss der Mutationen auf die Konformationsänderung und die Fusionsaktivität von HA wurden durch einen Proteinase K-Assay bzw. Fluoreszenzmikroskopie erfasst. Die Ergebnisse beider Methoden wurden miteinander korreliert. Abgesehen von der Mutante R109E zeigten Wildtyp-HA und alle anderen Mutanten eine vergleichbare ...
Successful infection by influenza virus requires that the envelope spike protein, hemagglutinin (HA), catalyzes fusion between the viral envelope and the intracellular endosomal membrane of the target cell and creates a pore large enough to release the viral genome. There is a growing appreciation that membrane lipids play a role in this critical event, coming mostly from experiments and theory on lipid composition in relationship to membrane monolayer curvature stress (Markin et al., 1984; Kozlov et al., 1989; Chizmadzhev et al., 1995; Chernomordik, 1996; Siegel, 1999; Kuzmin et al., 2001; Kozlovsky and Kozlov, 2003; Chernomordik et al., 2006). Recently there has been consideration given to the role of membrane phase behavior and membrane microdomains on the lateral distribution, sorting, and interactions of lipids with membrane proteins in general, and viral envelope glycoproteins in particular (Brown and London, 1998; Wang et al., 2001; Suomalainen, 2002; Chazal and Gerlier, 2003; Edidin, ...
mouse Anti-HA, conjugated to DyLight 550 antibodies, anti-HA conjugated to DyLight 550, directly conjugated anti-HA antibody, AS15 2920, Human influenza hemagglutinin (HA) tagged proteins
Influenza A virus H1 HA (Hemagglutinin) antibody [B219M] for ELISA, WB. Anti-Influenza A virus H1 HA (Hemagglutinin) mAb (GTX41203) is tested in Influenza A virus samples. 100% Ab-Assurance.
Influenza A virus H1 HA (Hemagglutinin) antibody [58CE8-1-5] for ICC/IF. Anti-Influenza A virus H1 HA (Hemagglutinin) mAb (GTX40266) is tested in Influenza A virus samples. 100% Ab-Assurance.
Recombinant H11N2 Hemagglutinin/HA Protein (Met1-Arg342) HA1 Subunit 11705-V08H1 with a fusion His Tag, is expressed in HEK293 Cells. With high purity, high biological activity, high stability, and other superior features, you can use this H11N2 Hemagglutinin/HA protein for relevant bioassay and related research.
Hemagglutinin consists of a globular head and a stem. The globular head consists of three chains, Chains A, C, and E. The stem of the protein consists of three chains as well, Chains B, D, and F.
The 12CA5 monoclonal antibody recognizes the 9-amino acid sequence YPYDVPDYA, derived from influenza virus hemagglutinin (HA). HA is commonly added to proteins of interest using recombinant DNA technology. The HA tag can then be used for detection or purification of the tagged protein.
Avian H7N9 influenza virus infection with fatal outcomes continues to pose a pandemic threat and highly immunogenic vaccines are urgently needed. In this report we show that baculovirus-derived recombinant H7 hemagglutinin protein, when delivered with RIG-I ligand, induced enhanced antibody and T cell responses and conferred protection against lethal challenge with a homologous H7N9 virus. These findings indicate the potential utility of RIG-I ligands as vaccine adjuvants to increase the immunogenicity of recombinant H7 hemagglutinin ...
HA Epitope Tag (YPYDVPDYA), 0.1 mg. Human influenza hemagglutinin (HA) is a surface glycoprotein required for the infectivity of the human virus.
HA Epitope Tag (YPYDVPDYA), 0.1 mg. Human influenza hemagglutinin (HA) is a surface glycoprotein required for the infectivity of the human virus.
Results show the strong anti-pain effect of HA vaccine (Table 5), which suggests that HA vaccine (anti-HA antibody) induced the neurogenesis of hippocampus; this suggestion is consistent with our observation that the hippocampal volume of the experimental mice is larger than that of the control mice ...
AlphaLISA Acceptor beads conjugated to anti-HA (hemagglutinin) antibody. These beads can be used to capture HA-tagged proteins and peptides.
TY - JOUR. T1 - Partitioning of proteins into plasma membrane microdomains. Clustering of mutant influenza virus hemagglutinins into coated pits depends on the strength of the internalization signal. AU - Fire, Ella. AU - Brown, Claire M.. AU - Roth, Michael G.. AU - Henis, Yoav I.. AU - Petersen, Nils O.. PY - 1997/11/21. Y1 - 1997/11/21. N2 - Internalization of membrane proteins involves their recruitment into plasma membrane clathrin-coated pits, with which they are thought to interact by binding to AP-2 adaptor protein complexes. To investigate the interactions of membrane proteins with coated pits at the cell surface, we applied image correlation spectroscopy to measure directly and quantitatively the clustering of influenza hemagglutinin (HA) protein mutants carrying specific cytoplasmic internalization signals. The HA system enables direct comparison between isolated internalization signals, because HA itself is excluded from coated pits. The studies presented here provide, for the first ...
cansSAR 3D Structure of 5VTQ_B | CRYSTAL STRUCTURE OF THE A/HONG KONG/1/1968 (H3N2) INFLUENZA VIRUS HEMAGGLUTININ G225L/L226S MUTANT IN COMPLEX WITH 3-SLN | 5VTQ
Playing Hide and Seek: How Glycosylation of the Influenza Virus Hemagglutinin Can Modulate the Immune Response to Infection. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
Influenza A and B viruses are major causes of seasonal flu epidemics each year. Hemagglutinin (HA) mediates the binding of virus to host cell and the fusion with host membrane. The crystal of HA in complex with antibody that reveals the mechanism by which antibody recognizes HA may not diffract to high resolution, thereby preventing the accurate interpretation of the structural model. The application of normal mode refinement that aims for improving the structure quality at the low resolution is tested. These studies provide some guidelines for future refinement of HA-antibody complex structures. By comparing the residues constituting the base of the receptor binding site of influenza A and B virus HAs, it is found that they share some similarities, except for a Phe at position 95 of influenza B virus hemagglutinin (BHA) versus Tyr in of influenza A virus hemagglutinin (AHA). The recombinant protein BHA containing the F95Y mutation exhibits the increased receptor binding affinity and ...
TY - JOUR. T1 - Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells. AU - Yoshimori, Tamotsu. AU - Keller, Patrick. AU - Roth, Michael G.. AU - Simons, Kai. PY - 1996/4. Y1 - 1996/4. N2 - The question of how membrane proteins are delivered from the TGN to the cell surface in fibroblasts has received little attention. In this paper we have studied how their post-Golgi delivery routes compare with those in epithelial cells. We have analyzed the transport of the vesicular stomatitis virus G protein, the Semliki Forest virus spike-glycoprotein, both basolateral in MDCK cells, and the influenza virus hemagglutinin, apical in MDCK cells. In addition, we also have studied the transport of a hemagglutinin mutant (Cys543Tyr) which is basolateral in MDCK cells. Aluminum fluoride, a general activator of heterotrimeric G proteins, inhibited the transport of the basolateral cognate proteins, as well as of the hemagglutinin mutant, from the TGN to the cell surface in BHK and ...
Influenza A virus (IAV) recognizes two types of N-acetylneuraminic acid (Neu5Ac) by galactose (Gal) linkages, Neu5Acα2,3Gal and Neu5Acα2,6Gal. Avian IAV preferentially binds to Neu5Acα2,3Gal linkage, while human IAV preferentially binds to Neu5Acα2,6Gal linkage, as a virus receptor. Shift in receptor binding specificity of avian IAV from Neu5Acα2,3Gal linkage to Neu5Acα2,6Gal linkage is generally believed to be a critical factor for its transmission ability among humans. Surveillance of this shift of highly pathogenic H5N1 avian IAV (HPAI) is thought to be a very important for prediction and prevention of a catastrophic pandemic of HPAI among humans. In this study, we demonstrated that receptor binding specificity of IAV bound to sialo-glycoconjugates was sensitively detected by quantifying the HA gene with real-time reverse-transcription-PCR. The new assay enabled direct detection of receptor binding specificity of HPAIs in chicken clinical samples including trachea and cloaca swabs in ...
Our structural and functional analyses suggest that H2 viruses of nonhuman origin readily adapted to human receptor specificity with only two mutations during the 1957 influenza pandemic. The conversion of binding specificity relies on precise interactions between HA and glycan receptors. A slight elongation of the binding pocket between H2-avian and H2-human, along with the hydrophobicity switch at residue 226, dictates drastically different glycan binding profiles. The seemingly stringent requirement for binding site length is suggested by the unique binding properties of the intermediate mutant H2-226L/228G. The intermediate mutant carries a leucine residue at position 226, the same as H2-human, yet still lacks binding affinities for α2,6-linked glycans. Preferential binding, thus, is achieved by exact positioning of interacting residues.. These structural comparisons elucidate the structural impact of the receptor-altering mutations Q226L/G228S at very high resolution. These three H2 ...
In article ,3hb70h$djn at charm.magnus.acs.ohio-state.edu,, tchang at magnus.acs.ohio-state.edu (Tien-Hsien Chang) writes: ,,,CUTS,,, , We would appreciate that someone can provide useful suggestions an/or , protocols regarding using anti-HA antibodies for this purpose in yeast. I , heard that anti-HA recognizes some related proteins in yeast cells. Is there a , way to get rid of these signals (we know of preadsorption by yeast powder may , help)? Pointers to references of using this approach in yeast are greatly , appreciated. , , , Tien-Hsien Chang , Assistant Professor , Department of Molecular Genetics , The Ohio State University , 484 West 12th Ave. , Columbus, OH 43210 , , (614)-292-0631 (phone) , (614)-292-4466 (fax) , chang.108 at osu.edu Tien-Hsien, My reply indicated all of the references used flu monoclonals described in the 1993 PNAS paper. I meant 1983 PNAS paper. I guess it just feels like yesterday,g,. Please let me know if any references are in error. Also let me know if there ...
Mouse monoclonal antibody raised against Influenza A Virus Haemagglutinin H5. Avian influenza virus type A (H5N1). (MAB3138) - Products - Abnova
Mouse monoclonal antibody raised against Influenza B virus hemagglutinin. B/Lee/40 and B/Singapore/-222/79 virus. (MAB14108) - Products - Abnova
We have examined human CD4+ T-cell recognition of influenza A/Beijing/32/92 (H3N2) virus hemagglutinin following influenza virus HANA subunit vaccination. CD4+ T-cell repertoires were dominated by recognition of epitopes located in conserved regions of the molecule, in a major histocompatibility complex class II haplotype-dependent manner, analogous to that observed following natural infection.. ...
Curlewis J.D., Clarke I.J. and McNeilly A.S. (1993) Dopamine D1 receptor analogues act centrally to stimulate prolactin secretion in ewes. Journal of Endocrinology, 137 3: 457-464. ...
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.
Infection with 2009 H1N1 pandemic influenza (pH1N1) boosted antibodies specific to the hemagglutinin (HA) stalk rather than its head, a phenomenon that may have contributed to the disappearance of seasonal H1N1 influenza strains circulating at the time, US researchers reported in a study in Proceedings of the National Academy of Sciences. The team created chimeric hemagglutinin (cHA) proteins and viruses expressing those chimeric proteins that allowed them to detect stalk-specific antibodies in preparations that also included head-specific antibodies. (The HA of flu viruses is shaped like a mushroom, with a head and a stalk.) They found relatively high titers of stalk-specific immunoglobulin G antibodies in the blood of pH1N1-infected patients compared with those who werent infected. By using cHA engineered with heads of viruses not seen in humans, the researchers showed the antibodies were reacting with the stalk and not the head. They also showed that the antibodies reduced virus replication. ...
Universal Fluhunter 2: Universal PCR kit for Hemagglutinin gene (HA-gene) decoding and detection of influenza viruses + 10 genesequencings
Figure 5. Binding of A/Taiwan/2/13 and the G225D mutant HA to biotinylated N‐glycan receptors, as determined by glycan ELISA. Wild‐type HA (upper panels) binds strongly to avian‐type receptors terminating in α2‐3 sialic acid (left, white open shapes) with weaker binding to human‐type (α2‐6) receptors (right, black closed shapes). Despite lower avidity, G225D (lower panels) shows strong human specificity, with slightly reduced binding to α2‐6 N‐glycans and no detectable interaction with avian receptors. Assays are conducted with biantennary, N‐linked glycans (N) with one to four LacNAc (LN, Galβ1‐4GlcNAc) repeats terminated with sialic acid (S) in α2‐3 or α2‐6 linkage (SLN1‐4‐N) (n = 2). An asialo, mono‐LacNAc (LacNAc‐biotin, LN‐L) was used as a negative binding control. ...
Hemagglutinin molecule of the H1 subtype from H1N1 swine flu virus, a type of influenza A virus. Hemagglutinin is a protein on the surface of the influenza virus that allows it to attach to host cells by binding to sialic acid residues on their cell membr - Stock Image C004/8948
I am looking for a source of Influenza virus haemagglutinin antigen. I need this to use as a positive control for westerns to check expression of a HA tagged protein. The antibody we are going to use is mAb 12CA5 (from Boehringer). I will appreciate if anyone in knowledge of the commercial availablility of the compatible HA antigen will give me the details of the source. Thanks very much Obaid Khan ...
Vaccine researchers have developed a strategy aimed at generating broadly cross-reactive antibodies against the influenza virus: embrace the unfamiliar.. In recent years, researchers interested in a "universal flu vaccine" identified a region of the viral hemagglutinin protein called the stem or stalk, which doesnt mutate and change as much as other regions and could be the basis for a vaccine that is protective against a variety of flu strains.. In an Emory Vaccine Center study, human volunteers immunized against the avian flu virus H5N1 readily developed antibodies against the stem region of the viral hemagglutinin protein. In contrast, those immunized with standard seasonal trivalent vaccines did not, instead developing most of their antibodies against the more variable head region. H5N1, regarded as a potential pandemic strain, is not currently circulating in the United States and the volunteers had not been exposed to it before.. The results were published Monday, August 25 in ...
Vaccine researchers have developed a strategy aimed at generating broadly cross-reactive antibodies against the influenza virus: embrace the unfamiliar.. In recent years, researchers interested in a "universal flu vaccine" identified a region of the viral hemagglutinin protein called the stem or stalk, which doesnt mutate and change as much as other regions and could be the basis for a vaccine that is protective against a variety of flu strains.. In an Emory Vaccine Center study, human volunteers immunized against the avian flu virus H5N1 readily developed antibodies against the stem region of the viral hemagglutinin protein. In contrast, those immunized with standard seasonal trivalent vaccines did not, instead developing most of their antibodies against the more variable head region. H5N1, regarded as a potential pandemic strain, is not currently circulating in the United States and the volunteers had not been exposed to it before.. The results were published Monday, August 25 in ...
Acid treatment of influenza A and B virus preparations followed by addition of dithiothreitol (DTT) and centrifugation through a sucrose cushion removes the HA1 subunit of hemagglutinin from virus. Rabbit sera made against these subviral particles and untreated virus were tested in a radioimmune pre …
If I understood correctly (and one of my own experiments suggests similarly), you should think of the TCR affinity scale as a sort of a slider: in one end you have high-affinity, microbe specific T cells (for example T cells specific for the influenza virus haemagglutinin have typically very high affinity), which are quickly able to initiate an immune response that eliminates the virus. However, these T cells lose their edge easily if the virus mutates. And somewhere in the middle of the scale you have T cells that have loose TCRs, which means that they are not very effective in eradicating the virus, but have a better chance to catch the mutant ones as well. However, with bad luck they can also recognize self antigens and initiate a response against own cells. In the other end you have TCRs that are more likely to recognize self antigens than foreign ones, and these are the ones that the body either tries to eliminate in the thymus or tries to turn into regulatory T cells that do not initiate ...
If I understood correctly (and one of my own experiments suggests similarly), you should think of the TCR affinity scale as a sort of a slider: in one end you have high-affinity, microbe specific T cells (for example T cells specific for the influenza virus haemagglutinin have typically very high affinity), which are quickly able to initiate an immune response that eliminates the virus. However, these T cells lose their edge easily if the virus mutates. And somewhere in the middle of the scale you have T cells that have loose TCRs, which means that they are not very effective in eradicating the virus, but have a better chance to catch the mutant ones as well. However, with bad luck they can also recognize self antigens and initiate a response against own cells. In the other end you have TCRs that are more likely to recognize self antigens than foreign ones, and these are the ones that the body either tries to eliminate in the thymus or tries to turn into regulatory T cells that do not initiate ...
Anti-Hemagglutinin/HA Antibody11713-T54, manufactured by Sino Biological is validated in WB,ELISA,FCM,ICC/IF,IP. Custom antibody services and bulk production also available. To learn more comprehensive our antibody product information including immunogen, specificity, and more, you can read all details here.
The news dribbling out about the sequencing of the Turkish isolates is not encouraging but also not surprising. As I noted several days ago, the proposition that the hemagglutinin protein of the isolates is "very close" to the avian sequences is not very informative because extremely small changes can cause important changes in host range, as studies by Stevens et al. on the 1918 HA show. That paper described studies with glycan arrays (see previous post) that looked at the binding of various viral HAs to various linkages of sialic acid, the cellular receptor. Sialic acid is linked in two forms, one characteristic of bird intestinal cells, one characteristic of human lower respiratory tract cells, although we now know that humans have avian-type linkages in sialic acid in their upper respiratory tract. Most avian viruses bind well to the avian receptor, human viruses to the human linked receptor, but the HA protein from a case from New Yorks second wave in the 1918 pandemic showed some affinity ...