Viral interference with antibody and complement
Identifieur interne : 000803 ( Istex/Corpus ); précédent : 000802; suivant : 000804Viral interference with antibody and complement
Auteurs : John Lubinski ; Thandavarayan Nagashunmugam ; Harvey M. FriedmanSource :
- 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
Links to Exploration step
ISTEX:BA059F63FBD497F5A824E755AC83A1B91DE35DB3Le document en format XML
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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. 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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.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>complement, complement regulatory proteins, Fc receptors, HSV-1, immune evasion</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1998">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-4VK6S18D-S/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier converted-article found"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla" xml:lang="en"><item-info><jid>YSCDB</jid><aid>90242</aid><ce:pii>S1084-9521(98)90242-7</ce:pii><ce:doi>10.1006/scdb.1998.0242</ce:doi><ce:copyright type="full-transfer" year="1998">Academic Press</ce:copyright></item-info><head><ce:dochead><ce:textfn>Regular Article</ce:textfn></ce:dochead><ce:title>Viral interference with antibody and complement</ce:title><ce:author-group><ce:author><ce:given-name>John</ce:given-name><ce:surname>Lubinski</ce:surname></ce:author><ce:author><ce:given-name>Thandavarayan</ce:given-name><ce:surname>Nagashunmugam</ce:surname></ce:author><ce:author><ce:given-name>Harvey M.</ce:given-name><ce:surname>Friedman</ce:surname></ce:author><ce:affiliation><ce:textfn>Division of Infectious Diseases, Department of Medicine, University of Pennsylvania School of Medicine, 536 Johnson Pavilion, Philadelphia, PA, 19104-6073, USA</ce:textfn></ce:affiliation></ce:author-group><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>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 virus<ce:italic>in vitro</ce:italic>and<ce:italic>in vivo</ce:italic>by inhibiting immune functions.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>complement, complement regulatory proteins, Fc receptors, HSV-1, immune evasion</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Viral interference with antibody and complement</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Viral interference with antibody and complement</title></titleInfo><name type="personal"><namePart type="given">John</namePart><namePart type="family">Lubinski</namePart><affiliation>Division of Infectious Diseases, Department of Medicine, University of Pennsylvania School of Medicine, 536 Johnson Pavilion, Philadelphia, PA, 19104-6073, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Thandavarayan</namePart><namePart type="family">Nagashunmugam</namePart><affiliation>Division of Infectious Diseases, Department of Medicine, University of Pennsylvania School of Medicine, 536 Johnson Pavilion, Philadelphia, PA, 19104-6073, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Harvey M.</namePart><namePart type="family">Friedman</namePart><affiliation>Division of Infectious Diseases, Department of Medicine, University of Pennsylvania School of Medicine, 536 Johnson Pavilion, Philadelphia, PA, 19104-6073, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1998</dateIssued><copyrightDate encoding="w3cdtf">1998</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract 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.</abstract><note type="content">Section title: Regular Article</note><subject lang="en"><genre>Keywords</genre><topic>complement, complement regulatory proteins, Fc receptors, HSV-1, immune evasion</topic></subject><relatedItem type="host"><titleInfo><title>Seminars in Cell and Developmental Biology</title></titleInfo><titleInfo type="abbreviated"><title>YSCDB</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1998</dateIssued></originInfo><identifier type="ISSN">1084-9521</identifier><identifier type="PII">S1084-9521(00)X0021-3</identifier><part><date>1998</date><detail type="volume"><number>9</number><caption>vol.</caption></detail><detail type="issue"><number>3</number><caption>no.</caption></detail><extent unit="issue-pages"><start>239</start><end>378</end></extent><extent unit="pages"><start>329</start><end>337</end></extent></part></relatedItem><identifier type="istex">BA059F63FBD497F5A824E755AC83A1B91DE35DB3</identifier><identifier type="ark">ark:/67375/6H6-4VK6S18D-S</identifier><identifier type="DOI">10.1006/scdb.1998.0242</identifier><identifier type="PII">S1084-9521(98)90242-7</identifier><accessCondition type="use and reproduction" contentType="copyright">©1998 Academic Press</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource><recordOrigin>Academic Press, ©1998</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-4VK6S18D-S/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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