Specificities of monoclonal and polyclonal antibodies that inhibit adsorption of herpes simplex virus to cells and lack of inhibition by potent neutralizing antibodies.
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Disulfide bond structure of glycoprotein D of herpes simplex virus types 1 and 2Pseudotyping of glycoprotein D-deficient herpes simplex virus type 1 with vesicular stomatitis virus glycoprotein G enables mutant virus attachment and entry.Soluble glycoprotein D blocks herpes simplex virus type 1 infection of rat eyes.Broad-spectrum inhibition of HIV-1 by a monoclonal antibody directed against a gp120-induced epitope of CD4.Directed selection of recombinant human monoclonal antibodies to herpes simplex virus glycoproteins from phage display librariesAnti-glycoprotein D antibodies that permit adsorption but block infection by herpes simplex virus 1 prevent virion-cell fusion at the cell surface.Recombinant human Fab to glycoprotein D neutralizes infectivity and prevents cell-to-cell transmission of herpes simplex viruses 1 and 2 in vitroInteraction of herpes simplex virus glycoprotein gC with mammalian cell surface moleculesCharacterization of cell-binding properties of bovine herpesvirus 1 glycoproteins B, C, and D: identification of a dual cell-binding function of gB.The receptor-binding domain of pseudorabies virus glycoprotein gC is composed of multiple discrete units that are functionally redundant.Specificity and affinity of binding of herpes simplex virus type 2 glycoprotein B to glycosaminoglycans.Antibody raised against soluble CD4-rgp120 complex recognizes the CD4 moiety and blocks membrane fusion without inhibiting CD4-gp120 binding.Use of lambda gt11 to isolate genes for two pseudorabies virus glycoproteins with homology to herpes simplex virus and varicella-zoster virus glycoproteinsExpression of seven herpes simplex virus type 1 glycoproteins (gB, gC, gD, gE, gG, gH, and gI): comparative protection against lethal challenge in mice.Swine testis cells contain functional heparan sulfate but are defective in entry of herpes simplex virus.Herpes simplex virus type 1-induced hemagglutination: glycoprotein C mediates virus binding to erythrocyte surface heparan sulfateBovine herpesvirus 1 attachment to permissive cells is mediated by its major glycoproteins gI, gIII, and gIV.Expression of a human cytomegalovirus receptor correlates with infectibility of cells.Herpes simplex virus glycoprotein D mediates interference with herpes simplex virus infectionCysteine mutants of herpes simplex virus type 1 glycoprotein D exhibit temperature-sensitive properties in structure and function.Absence of asparagine-linked oligosaccharides from glycoprotein D of herpes simplex virus type 1 results in a structurally altered but biologically active protein.Interaction of glycoprotein gIII with a cellular heparinlike substance mediates adsorption of pseudorabies virusDeletions in herpes simplex virus glycoprotein D define nonessential and essential domains.Soluble forms of herpes simplex virus glycoprotein D bind to a limited number of cell surface receptors and inhibit virus entry into cells.Entry of herpes simplex virus 1 in BJ cells that constitutively express viral glycoprotein D is by endocytosis and results in degradation of the virusSynthesis, cellular location, and immunogenicity of bovine herpesvirus 1 glycoproteins gI and gIII expressed by recombinant vaccinia virusFine mapping of antigenic site II of herpes simplex virus glycoprotein DNeutralizing antibodies specific for glycoprotein H of herpes simplex virus permit viral attachment to cells but prevent penetrationInfluence of asparagine-linked oligosaccharides on antigenicity, processing, and cell surface expression of herpes simplex virus type 1 glycoprotein D.Pathogenicity in mice of herpes simplex virus type 2 mutants unable to express glycoprotein CA herpes simplex virus mutant in which glycoprotein D sequences are replaced by beta-galactosidase sequences binds to but is unable to penetrate into cells.Expression of herpes simplex virus type 1 glycoprotein D deletion mutants in mammalian cellsThe contribution of cysteine residues to antigenicity and extent of processing of herpes simplex virus type 1 glycoprotein DA monoclonal antibody to glycoprotein gp85 inhibits fusion but not attachment of Epstein-Barr virus.Soluble gp350/220 and deletion mutant glycoproteins block Epstein-Barr virus adsorption to lymphocytes.Herpes simplex viruses lacking glycoprotein D are unable to inhibit virus penetration: quantitative evidence for virus-specific cell surface receptors.C3b receptor activity on transfected cells expressing glycoprotein C of herpes simplex virus types 1 and 2.Expression of bovine herpesvirus 1 glycoproteins gI and gIII in transfected murine cells.Localization of discontinuous epitopes of herpes simplex virus glycoprotein D: use of a nondenaturing ("native" gel) system of polyacrylamide gel electrophoresis coupled with Western blottingPotent neutralizing activity associated with anti-glycoprotein D specificity among monoclonal antibodies selected for binding to herpes simplex virions.
P2860
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P2860
Specificities of monoclonal and polyclonal antibodies that inhibit adsorption of herpes simplex virus to cells and lack of inhibition by potent neutralizing antibodies.
description
1985 nî lūn-bûn
@nan
1985年の論文
@ja
1985年論文
@yue
1985年論文
@zh-hant
1985年論文
@zh-hk
1985年論文
@zh-mo
1985年論文
@zh-tw
1985年论文
@wuu
1985年论文
@zh
1985年论文
@zh-cn
name
Specificities of monoclonal an ...... otent neutralizing antibodies.
@en
type
label
Specificities of monoclonal an ...... otent neutralizing antibodies.
@en
prefLabel
Specificities of monoclonal an ...... otent neutralizing antibodies.
@en
P2860
P1433
P1476
Specificities of monoclonal an ...... potent neutralizing antibodies
@en
P2093
P2860
P304
P407
P577
1985-08-01T00:00:00Z