Mouse Monoclonal Anti-Respiratory Syncytial Virus fusion protein Antibody (10B6) [DyLight 488]. Validated: ELISA, Flow. Tested Reactivity: Virus. 100% Guaranteed.
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The fusion (F) and hemagglutinin-neuraminidase (HN) glycoproteins of the paramyxovirus simian virus 5 (SV5) were expressed individually or coexpressed in CV-1 cells by using SV40-based vectors and recombinant vaccinia viruses. The extent of detectable fusion in a syncytium formation assay was found to be affected by the expression system used. In addition, when HN was coexpressed with F, it was found that the expression vector system influenced the contribution of HN in forming syncytia. The abilities of the SV5, human parainfluenza virus type 3, and Newcastle disease virus F glycoproteins to cause fusion, when expressed alone or coexpressed with HN, were directly compared by using the SV40-based vector system in CV-1 cells. The F proteins exhibited various degrees of fusion activity independent of HN expression, but the formation of syncytia could be enhanced to different extents by the coexpression of the homotypic HN protein. ...
Coronaviruses are enveloped positive-stranded RNA viruses that replicate in the cytoplasm. To deliver their nucleocapsid into the host cell, they rely on the fusion of their envelope with the host cell membrane. The spike glycoprotein (S) mediates virus entry and is a primary determinant of cell tropism and pathogenesis. It is classified as a class I fusion protein, and is responsible for binding to the receptor on the host cell as well as mediating the fusion of host and viral membranes-A process driven by major conformational changes of the S protein. This review discusses coronavirus entry mechanisms focusing on the different triggers used by coronaviruses to initiate the conformational change of the S protein: receptor binding, low pH exposure and proteolytic activation. We also highlight commonalities between coronavirus S proteins and other class I viral fusion proteins, as well as distinctive features that confer distinct tropism, pathogenicity and host interspecies transmission characteristics
3RRT: Structure of respiratory syncytial virus fusion glycoprotein in the postfusion conformation reveals preservation of neutralizing epitopes.
Lysolipids added between fusing membranes inhibit and cis-unsaturated fatty acids promote not only diverse biological fusion reactions (this paper and Creutz, 1981; Glick and Rothman, 1987; Chernomordik et al., 1993; Paiement et al., 1994; Yeagle et al., 1994; Chernomordik et al., 1995c; Gunther-Ausborn et al., 1995; but see Nagao et al., 1995; Coorssen, 1996), but also fusion of purely lipid bilayers (for review see Chernomordik et al., 1995b). Importantly, LPC inhibits HA-mediated fusion at membrane concentrations similar to those found to inhibit syncytia formation mediated by the Sendai virus F protein (Yeagle et al., 1994) and baculovirus gp64 (Chernomordik et al., 1995c), as well as for microsome-microsome fusion (Chernomordik et al., 1993) and vesicle-planar bilayer fusion (Chernomordik et al., 1995a). We suggest that fusion mediated by HA and other proteins and fusion of purely lipid bilayers proceed via a common lipid-involving intermediate-a stalk structure, producing local and ...
casSAR Dugability of P17003 | HE | Hemagglutinin-esterase-fusion glycoprotein - Also known as HEMA_INCHY, HE. Binds to the N-acetyl-9-O-acetylneuraminic acid residues on the cell surface, bringing about the attachment of the virus particle to the cell. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induce an irreversible conformational change in HEF2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. Displays a receptor-destroying activity which is a neuraminidate-O-acetyl esterase. This activity cleaves off any receptor on the cell surface, which would otherwise prevent virions release. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell (By
The long-term goal of the proposed research is to understand the basis for viral fusion protein-induced membrane fusion with atomic-resolution detail. Fusion of...
DI-fusion, le Dépôt institutionnel numérique de lULB, est loutil de référencementde la production scientifique de lULB.Linterface de recherche DI-fusion permet de consulter les publications des chercheurs de lULB et les thèses qui y ont été défendues.
3O45: Structure of a Major Antigenic Site on the Respiratory Syncytial Virus Fusion Glycoprotein in Complex with Neutralizing Antibody 101F.
To infect host cells, most enveloped viruses must insert a hydrophobic fusion peptide into the host cell membrane. Thus, fusion peptides may be valuable targets for developing drugs that block virus entry. We have shown previously that a natural 20-residue fragment of α1-antitrypsin, designated VIRus-Inhibitory Peptide (VIRIP), that binds to the gp41 fusion peptide of HIV-1 prevents the virus from entering target cells in vitro. Here, we examine the efficacy of 10-day monotherapy with the optimized VIR-576 derivative of VIRIP in treatment-naïve, HIV-1-infected individuals with viral RNA loads of ≥10,000 copies per ml. We report that at the highest dose (5.0 grams per day), intravenous infusion of VIR-576 reduced the mean plasma viral load by 1.23 log10 copies per ml without causing severe adverse effects. Our results are proof of concept that fusion peptide inhibitors suppress viral replication in human patients, and offer prospects for the development of a new class of drugs that prevent ...
Enveloped viruses enter cells by using their fusion proteins to merge the virus lipid envelope and the cell membrane. While crystal structures of the water-soluble ectodomains of many viral fusion proteins have been determined, the structure and assembly of the C-terminal transmembrane domain (TMD) remains poorly understood. Here we use solid-state NMR to determine the backbone conformation and oligomeric structure of the TMD of the parainfluenza virus 5 (PIV5) fusion protein. 13C chemical shifts indicate that the central leucine-rich segment of the TMD is α-helical in POPC/cholesterol membranes and POPE membranes, while the Ile- and Val-rich termini shift to the β-strand conformation in the POPE membrane ...
Enveloped viruses enter cells by using their fusion proteins to merge the virus lipid envelope and the cell membrane. While crystal structures of the water-soluble ectodomains of many viral fusion proteins have been determined, the structure and assembly of the C-terminal transmembrane domain (TMD) remains poorly understood. Here we use solid-state NMR to determine the backbone conformation and oligomeric structure of the TMD of the parainfluenza virus 5 (PIV5) fusion protein. 13C chemical shifts indicate that the central leucine-rich segment of the TMD is α-helical in POPC/cholesterol membranes and POPE membranes, while the Ile- and Val-rich termini shift to the β-strand conformation in the POPE membrane ...
article{1942045, abstract = {Despite the medical importance of respiratory syncytial virus (RSV) infections, there is no vaccine or therapeutic agent available. Prophylactic administration of palivizumab, a humanized monoclonal RSV fusion (F) protein-specific antibody, can protect high-risk children. Previously, we have demonstrated that RSV can be neutralized by picomolar concentrations of a camelid immunoglobulin single-variable domain that binds the RSV protein F (F-VHHb nanobodies). Here, we investigated the mechanism by which these nanobodies neutralize RSV and tested their antiviral activity in vivo. We demonstrate that bivalent RSV F-specific nanobodies neutralize RSV infection by inhibiting fusion without affecting viral attachment. The ability of RSV F-specific nanobodies to protect against RSV infection was investigated in vivo. Intranasal administration of bivalent RSV F-specific nanobodies protected BALB/c mice from RSV infection, and associated pulmonary inflammation. Moreover, ...
Binds to the N-acetyl-9-O-acetylneuraminic acid residues on the cell surface, bringing about the attachment of the virus particle to the cell. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induce an irreversible conformational change in HEF2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. Displays a receptor-destroying activity which is a neuraminidate-O-acetyl esterase. This activity cleaves off any receptor on the cell surface, which would otherwise prevent virions release. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell (By similarity).
Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization either through clathrin-dependent endocytosis or through clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.
Common themes are emerging from the study of viral, cell-cell, intracellular, and liposome fusion. Viral and cellular membrane fusion events are mediated by fusion proteins or fusion machines. Viral fusion proteins share important characteristics, notably a fusion peptide within a transmembrane-anchored polypeptide chain. At least one protein involved in a cell-cell fusion reaction resembles viral fusion proteins. Components of intracellular fusion machines are utilized in multiple membrane trafficking events and are conserved through evolution. Fusion pores develop during and intracellular fusion events suggesting similar mechanisms for many, if not all, fusion events. ...
Experimental evidence points towards a remarkably conserved mechanism by which virally encoded envelope glycoproteins catalyse membrane fusion and facilitate delivery of the viral core into the target cell [13, 14]. The structures of several class 1 fusion proteins reveal a characteristic "trimer-of-hairpins" motif believed to represent a late or post-fusion conformation [16-19, 35-37]. Investigating the way in which envelope proteins fold from a rod-like, pre-hairpin intermediate into the trimer-of-hairpins to pull the viral and cellular membranes together is important not only for our understanding of viral entry but also for the development of therapeutically relevant inhibitors of this process.. The protein sequences of the TM ectodomains of BLV and HTLV-1 display a striking level of conservation. By scrutinizing the position of conserved residues in the context of the HTLV-1 six-helix-bundle structure, we have found that the majority of the conserved residues map to the interacting surfaces ...
Single-particle studies of dengue-virus membrane fusion and the effect of small-molecule inhibitors of infection clarify the viral fusion mechanism.
In this study, we demonstrate that cytokines induce 1) dephosphorylation of Bad on Ser136 in INS-1 and rat islet cells, 2) Bax-dependent release of cytochrome c and inhibition of mitochondrial metabolic activity in human islets, 3) cleavage/activation of caspase-9 in INS-1 cells and rat islets and cleavage/activation of caspase-3 in INS-1 cells and rat and human islets, and finally 4) β-cell apoptosis in INS-1 cells and rat and human islets. Taken together, our findings strongly suggest that cytokines induce β-cell apoptosis through the canonical intrinsic mitochondrial pathway.. It has been suggested that cytokine-induced β-cell death is independent of Bax or Bak since siRNA-mediated knockdown of Bax or Bak failed to affect cytokine-induced cell death (39). In that study, the combination of IL-1β and IFN-γ was found to induce cell death in INS-1-derived cell lines and rat islets via nonapoptotic killing, which is in contrast to our present observations. However, the INS-1-derived cells ...
E1 is a class II viral fusion protein. This trimeric (low-pH-iduced) form is fusion active, and promotes release of viral nucleocapsid in cytoplasm after cell and viral membrane fusion. Efficient fusion requires the presence of cholesterol and sphingolipid in the target membrane. N-terminal domain of this protein: 1dyl(NMR), 1vcp, 1vcq ...
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Newcastle disease virus (NDV) causes severe diseases in avian species. Its fusion protein cleavage site (Fcs) is a major contributor to virulence and membrane fusion. Previous studies showed that a change from phenylalanine (F) to lysine (L) at position 117 of the virulent strain fusion protein, which has the polybasic amino acid Fcs motif
The data presented here provide functional evidence that a highly conserved loop at the tip of each subunit of the flavivirus E protein is important for fusion activity and may be directly involved in interactions with target membranes during the initial stages of membrane fusion. The notion that this portion of the protein serves as an internal fusion peptide is consistent with earlier observations that antipeptide antibodies recognizing the region from amino acids 98 to 110 are capable of blocking low-pH-induced fusion of TBE virus with artificial membranes (47) and react more strongly with the low-pH form of the dengue 2 virus E protein than with the native neutral form (40). We have recently observed that the flavivirus cross-reactive MAb A1, whose binding was shown in the present study to be abolished by amino acid substitutions at Leu 107, is also capable of inhibiting virus-liposome fusion and binding of isolated E proteins to artificial membranes (K. Stiasny et al., unpublished data). ...
The G2 fusion subunit of the Junin virus envelope glycoprotein GP-C contains two hydrophobic heptad-repeat regions that are postulated to form a six-helix bundle structure required for the membrane fusion activity of Class I viral fusion proteins. We have investigated the role of these heptad-repeat regions and, specifically, the importance of the putative interhelical a and d position sidechains by using alanine-scanning mutagenesis. All the mutant glycoproteins were expressed and transported to the cell surface. Proteolytic maturation at the subtilisin kexin isozyme-1/site-1-protease (SKI-1/S1P) cleavage site was observed in all but two of the mutants. Among the adequately cleaved mutant glycoproteins, four positions in the N-terminal region (I333, L336, L347 and L350) and two positions in the C-terminal region (R392 and W395) were shown to be important determinants of cell-cell fusion. Taken together, our results indicate that {alpha}-helical coiled-coil structures are likely critical in ...
Protein-mediated membrane fusion is essential for maintaining eukaryotic cell organization and propagation of major human viruses. Many clinically relevant memb...
You achieved immediate and lasting fame with your novel about the plain but spirited governess, Jane Eyre. The only Bronte sibling to marry, you outlived your brother and sisters, and, unlike Anne and Emily, had a chance to enjoy your celebrity and meet other authors of your day. However, you died in early pregnancy before you were forty ...
Antiviral blocking peptides targeting the viral fusion core can inhibit viral membrane fusion, thereby inhibiting the viruss entry into the host cell.
The retroviral envelope-derived proteins syncytin-1 and syncytin-2 (syn1 and syn2) drive placentation in humans by forming a syncytiotophoblast, a structure
Fooling the Virus: The Fusion protein as Virus-Specific Therapeutic An ACE2 A fusion protein of ACE2 with an Immunogenic Component Project ID : 47-2020-10877
IFITM-mediated restriction of virus-endosome fusion in different cell types.(A) IFITM3-mediated inhibition of viral fusion with different cell types. BlaM-Vpr c
Complete information for CACNA1F gene (Protein Coding), Calcium Voltage-Gated Channel Subunit Alpha1 F, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
C9orf125 human Fusion Protein GST from Proteintech. Produced in E.coli-derived, PET28a, with high quality purity. Cat.No. Ag14695
P27; KIP1 human Fusion Protein GST from Proteintech. Produced in E.coli-derived, PET28a, with high quality purity. Cat.No. Ag2280
Aguilar, P.S., Baylies, M.K., Fleissner, A., Helming, L., Inoue, N., Podbilewicz, B., Wang, H., and Wong, M. (2013). Genetic basis of cell-cell fusion mechanisms. Trends in genetics : TIG 29, 427-437 ...
In a previous study we demonstrated that vesicular stomatitis virus (VSV) can be used as a vector to express a soluble protein in mammalian cells. Here we have generated VSV recombinants that express four different membrane proteins: the cellular CD4 protein, a CD4-G hybrid protein containing the ectodomain of CD4 and the transmembrane and cytoplasmic tail of the VSV glycoprotein (G), the measles virus hemagglutinin, or the measles virus fusion protein. The proteins were expressed at levels ranging from 23-62% that of VSV G protein and all were transported to the cell surface. In addition we found that all four proteins were incorporated into the membrane envelope of VSV along with the VSV G protein. The levels of incorporation of these proteins varied from 6-31% of that observed for VSV G. These results suggest that many different membrane proteins may be co-incorporated quite efficiently with VSV G protein into budding VSV virus particles and that specific signals are not required for this ...
In molecular biology, haemagglutinin-esterase fusion glycoprotein (HEF) is a multi-functional protein embedded in the viral envelope of several viruses, including influenza C virus, coronaviruses and toroviruses. HEF is required for infectivity, and functions to recognise the host cell surface receptor, to fuse the viral and host cell membranes, and to destroy the receptor upon host cell infection. The haemagglutinin region of HEF is responsible for receptor recognition and membrane fusion, and bears a strong resemblance to the sialic acid-binding haemagglutinin found in influenza A and B viruses, except that it binds 9-O-acetylsialic acid. The esterase region of HEF is responsible for the destruction of the receptor, an action that is carried out by neuraminidase in influenza A and B viruses. The esterase domain is similar in structure to Streptomyces scabies esterase, and to acetylhydrolase, thioesterase I and rhamnogalacturonan acetylesterase. The haemagglutinin-esterase glycoprotein HEF must ...
Newcastle disease (ND) is regarded as a highly contagious and economically important disease in poultry and has a worldwide distribution. Viral determinants for Newcastle disease virus (NDV) virulence are not completely understood and viruses of different pathotypes can be found at live-bird markets in different geographical areas. The prevalence of Newcastle disease in village poultry in Mozambique is not well documented and strains of NDV involved in yearly outbreaks are unknown. The fusion (F) protein is an important determinant of pathogenicity of the virus and is used commonly for phylogenetic analysis. Newcastle disease viruses from various geographical regions of Mozambique were sequenced and compared genetically to published sequences obtained from GenBank. Samples were collected in three different areas of Mozambique and NDV was isolated by infection of embryonated chicken eggs. Sequence analysis of the F-protein encoding gene was used to classify 28 isolates from Mozambique into ...
The use of the insect virus Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV) as a gene delivery vector for mammalian cells began in 1995 with the discovery that mammalian hepatocytes could be efficiently infected by the virus (40). Since then, its use has increased steadily as a result of the number of advantages the system confers: an inability to replicate in mammalian cells or cause cellular toxicity, efficient entry in certain cell lines, inherent flexibility of use and additional benefits specific to the transient expression of drug targets. However, the system has retained the limitation of inefficient entry into some mammalian cells, limiting the usefulness of the system to particular cell lines. To improve the breadth of mammalian cell entry exhibted by AcMNPV the mechanisms of promiscuous cell entry were investigated. Initial results revealed that simple physical and chemical techniques such as using low pH diluents, optimising transduction volumes and increasing access ...
Read "Pathotyping isolates of Newcastle disease virus using antipeptide antibodies to pathotype-specific regions of their fusion and hemagglutinin-neuraminidase proteins, Archives of Virology" on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
The precise way in which the presence of NDV induces tumor cell death remains to be clarified and may show variation regarding the strains of NDV used and which type of cancer is targeted. NDV triggers apoptosis[17] in a wide range of cancer cell types via the mitochondrial/intrinsic pathway, through loss of membrane potential and thereby inducing release of cytochrome c in the tumor cell. The results[17] also indicate the extrinsic pathway is activated by TNF-related, apoptosis-inducing ligand-induced, NDV-mediated apoptosis in a late stage. Another study[20] found a hyperfusogenic NDV/F3aa(L289A) with refined abilities to fuse into somatic cells. NDV has aggregating properties causing syncytia formations of tumor cells, which, apart from amplifying immune-based cell killing, also results in necrosis of cells. This pathway was believed to lead to a considerable boost of immune activation and potentially an antitumor response, which was supported by observations of a significant accumulation of ...
Mumps is caused by a paramyxovirus with a negative-strand, nonsegmented RNA genome of 15,384 bases encoding at least 8 proteins: the nucleo- (N), phospho- (P), V, matrix (M), fusion (F), small hydrophobic (SH), hemagglutinin-neuraminidase (HN), and large (L) proteins. The N, P, and L proteins together provide the polymerase activity responsible for genome transcription and replication. The viral genome is surrounded by a host cell-derived lipid bilayer envelope containing the M, F, SH, and HN proteins. The M protein is involved in viral assembly, whereas the HN and F proteins are responsible for cell attachment and entry and are the major targets of virus-neutralizing antibody. The V and SH proteins are accessory proteins, acting as antagonists of the host antiviral response; the former interferes with the interferon response and the latter with the tumor necrosis factor α (TNF-α)-mediated apoptotic signaling pathway. Because of the hypervariability of the SH gene, its nucleotide sequence is ...
Virus-cell and cell-cell fusion.: Significant progress has been made in elucidating the mechanisms of viral membrane fusion proteins; both those that function a
multiple nucleopolyhedrovirus (AcMNPV), a known person in the sort We alphabaculoviruses, can transduce and deliver an operating gene to a variety of non-host cells, including many mammalian lines and major cells, a house mediated from the envelope fusion proteins GP64. appealing cell-targeting features. By seamlessly swapping the indigenous coding series with each of five sequences encoding different F protein, a couple of F-pseudotyped AcMNPV was produced. This report information their relative capabilities both to functionally replace GP64 in viral development also to transduce human being Saos-2 and HeLa cells. All Rabbit Polyclonal to KLRC1 five backed viable attacks in insect cell ethnicities and one, the NPV (MacoNPV) F pseudotype, could be amplified to titres close to those of native AcMNPV. In contrast, none was able to transduce the Saos-2 and HeLa cell lines. The strong support provided by MacoNPV F in computer virus production makes the corresponding pseudotype a viable scaffold to ...
An analysis of the R18 fusion assay was made during the fusion of the Sendai virus with erythrocyte ghosts. The increase in R18 fluorescence, reflecting the interaction process, was evaluated in terms of the different processes that in principle may contribute to this increase, that is, monomeric probe transfer, hemifusion, and complete fusion. To this end, the kinetics of the R18-labeled lipid mixing were compared to those obtained with an assay in which the fusion-monitoring probe, eosin-maleimide, was attached to the viral surface proteins. The experiments relied on the use of native and fusion-inactive viruses and studies involving viral and target membranes that were modified by the incorporation of the lysophospholipid. The total dequenching signal detected in the R18 assay consists of components from probe transferred without fusion and from fusion itself. At 37 degrees C, the initial rate of dequenching (within two minutes) was predominately from the probe diluted by fusion with little
Complete information for NUTM2F gene (Protein Coding), NUT Family Member 2F, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
HIV-1 enters its target cells by fusion at the plasma membrane. The primary cellular receptor for HIV is CD4, but this molecule is insufficient to permit viral fusion. During 1996, the necessary entry co-factors (co-receptors or second receptors) were identified as being members of the seven-transme …
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Human metapneumovirus (HMPV) is a leading cause of respiratory infection that causes upper airway and severe lower respiratory tract infections. HMPV infection is initiated by viral surface glycoproteins that attach to cellular receptors and mediate virus membrane fusion with cellular membranes. Most paramyxoviruses use two viral glycoproteins to facilitate virus entry-an attachment protein and a fusion (F) protein. However, membrane fusion for the human paramyxoviruses in the Pneumovirus subfamily, HMPV and respiratory syncytial virus (hRSV), is unique in that the F protein drives fusion in the absence of a separate viral attachment protein. Thus, pneumovirus F proteins can perform the necessary functions for virus entry, i.e., attachment and fusion. In this review, we discuss recent advances in the understanding of how HMPV F mediates both attachment and fusion. We review the requirements for HMPV viral surface glycoproteins during entry and infection, and review the identification of cellular
TY - JOUR. T1 - The secreted g protein of human respiratory syncytial virus antagonizes antibody-mediated restriction of replication involving macrophages and complement. AU - Bukreyev, Alexander. AU - Yang, Lijuan. AU - Collins, Peter L.. PY - 2012/10/1. Y1 - 2012/10/1. N2 - The respiratory syncytial virus (RSV) G and F glycoproteins are the neutralization antigens, and G also is expressed in a soluble form (sG). Previously, sG was demonstrated to reduce the efficiency of RSV antibody-mediated neutralization by serving as an antigen decoy and to inhibit the antibody-mediated antiviral effects of Fc receptor-bearing leukocytes. The present study demonstrated that effective antibody-mediated restriction in vivo, and the evasion of this restriction by sG, involves pulmonary macrophages and complement, but not neutrophils.. AB - The respiratory syncytial virus (RSV) G and F glycoproteins are the neutralization antigens, and G also is expressed in a soluble form (sG). Previously, sG was demonstrated ...