Viral interference with antibody and complement
Identifieur interne : 000770 ( Istex/Curation ); précédent : 000769; suivant : 000771Viral interference with antibody and complement
Auteurs : John Lubinski [États-Unis] ; Thandavarayan Nagashunmugam [États-Unis] ; Harvey M. Friedman [États-Unis]Source :
- Seminars in Cell and Developmental Biology [ 1084-9521 ] ; 1998.
English descriptors
- KwdEn :
- Teeft :
- Amino, Amino acid, Amino acids, Antibody bipolar, Basu, Binding activity, Binding proteins, Cascade, Chain subunit, Cohen, Complement activation, Complement activity, Complement cascade, Cysteine, Disulfide, Domain, Dubin, Eisenberg, Encodes, Evasion, Extracellular, Extracellular domain, Extracellular domains, Fcyr, Fcyr activity, Fcyrs, Friedman, Glycoprotein, Herpes, Herpes simplex virus, Herpes simplex virus glycoprotein, Herpes simplex virus type, Herpes simplex virus types, Herpesvirus, Herpesvirus saimiri, Homology, Immune, Immune evasion, Immunoglobulin, Immunol, Lubinski, Lysis, Membrane attack, Mouse hepatitis virus, Mutant, Mutant virus, Peplomer protein, Peptide, Potential glycosylation sites, Receptor, Simplex, Third component, Transmembrane domain, Vaccinia, Viral, Virion, Virol, Virology, Virus.
Abstract
Abstract: Viruses have evolved strategies to evade immunity mediated by antibody and complement. Herpesviruses and coronaviruses encode IgG Fc binding proteins that inhibit IgG activity, enabling the virus or infected cell to escape antibody attack. Herpesviruses, vaccinia virus and HIV-1 have the capacity to interfere with complement, either by incorporation of cellular complement regulatory proteins into the virion envelope or cell membrane, or by expression of viral molecules that mimic functions of complement regulatory proteins. The structure and biological activities of herpes simplex virus type 1 (HSV-1) glycoproteins gE, gI and gC are described. These glycoproteins protect HSV from immune attack; HSV-1 gE/gI form a complex that binds the Fc domain of IgG while gC is a C3b binding complement regulatory protein, providing a survival advantage to the virusin vitroandin vivoby inhibiting immune functions.
Url:
DOI: 10.1006/scdb.1998.0242
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Friedman</name><affiliation wicri:level="1"><mods:affiliation>Division of Infectious Diseases, Department of Medicine, University of Pennsylvania School of Medicine, 536 Johnson Pavilion, Philadelphia, PA, 19104-6073, USA</mods:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Division of Infectious Diseases, Department of Medicine, University of Pennsylvania School of Medicine, 536 Johnson Pavilion, Philadelphia, PA, 19104-6073</wicri:regionArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Seminars in Cell and Developmental Biology</title><title level="j" type="abbrev">YSCDB</title><idno type="ISSN">1084-9521</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1998">1998</date><biblScope unit="volume">9</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="329">329</biblScope><biblScope unit="page" to="337">337</biblScope></imprint><idno type="ISSN">1084-9521</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1084-9521</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>complement, complement regulatory proteins, Fc receptors, HSV-1, immune evasion</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Amino</term><term>Amino acid</term><term>Amino acids</term><term>Antibody bipolar</term><term>Basu</term><term>Binding activity</term><term>Binding proteins</term><term>Cascade</term><term>Chain subunit</term><term>Cohen</term><term>Complement activation</term><term>Complement activity</term><term>Complement cascade</term><term>Cysteine</term><term>Disulfide</term><term>Domain</term><term>Dubin</term><term>Eisenberg</term><term>Encodes</term><term>Evasion</term><term>Extracellular</term><term>Extracellular domain</term><term>Extracellular domains</term><term>Fcyr</term><term>Fcyr activity</term><term>Fcyrs</term><term>Friedman</term><term>Glycoprotein</term><term>Herpes</term><term>Herpes simplex virus</term><term>Herpes simplex virus glycoprotein</term><term>Herpes simplex virus type</term><term>Herpes simplex virus types</term><term>Herpesvirus</term><term>Herpesvirus saimiri</term><term>Homology</term><term>Immune</term><term>Immune evasion</term><term>Immunoglobulin</term><term>Immunol</term><term>Lubinski</term><term>Lysis</term><term>Membrane attack</term><term>Mouse hepatitis virus</term><term>Mutant</term><term>Mutant virus</term><term>Peplomer protein</term><term>Peptide</term><term>Potential glycosylation sites</term><term>Receptor</term><term>Simplex</term><term>Third component</term><term>Transmembrane domain</term><term>Vaccinia</term><term>Viral</term><term>Virion</term><term>Virol</term><term>Virology</term><term>Virus</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Viruses have evolved strategies to evade immunity mediated by antibody and complement. Herpesviruses and coronaviruses encode IgG Fc binding proteins that inhibit IgG activity, enabling the virus or infected cell to escape antibody attack. Herpesviruses, vaccinia virus and HIV-1 have the capacity to interfere with complement, either by incorporation of cellular complement regulatory proteins into the virion envelope or cell membrane, or by expression of viral molecules that mimic functions of complement regulatory proteins. The structure and biological activities of herpes simplex virus type 1 (HSV-1) glycoproteins gE, gI and gC are described. These glycoproteins protect HSV from immune attack; HSV-1 gE/gI form a complex that binds the Fc domain of IgG while gC is a C3b binding complement regulatory protein, providing a survival advantage to the virusin vitroandin vivoby inhibiting immune functions.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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