Herpes Simplex Virus (HSV) Glycoproteins B and K Inhibit Cell Fusion Induced by HSV Syncytial Mutants
Identifieur interne : 002712 ( Istex/Corpus ); précédent : 002711; suivant : 002713Herpes Simplex Virus (HSV) Glycoproteins B and K Inhibit Cell Fusion Induced by HSV Syncytial Mutants
Auteurs : Lloyd Hutchinson ; Frank L. Graham ; Weizhong Cai ; Chitrita Debroy ; Stanley Person ; David C. JohnsonSource :
- Virology [ 0042-6822 ] ; 1993.
Abstract
Abstract: Herpes simplex virus type 1 (HSV-1) glycoproteins K and B (gK and gB) are intimately involved in virus-induced fusion of cells. Certain mutations in the UL27 (gB) and UL53 (gK) genes confer a syncytial (syn) phenotype characterized by extensive fusion of infected cells and giving rise to multinucleated cells. We have used HSV-1 syn mutants in conjunction with transfected cells or adenovirus vectors to overexpress wild-type gK or gB, in order to study the role of these proteins in virus-induced membrane fusion. Transient expression of wild-type gK inhibited fusion induced by HSV-1 encoding a mutant form of gK (syn gK) but not by viruses encoding a mutant form of gB (syn gB). Stably transformed cells expressing relatively high levels of gK suppressed cell fusion induced by HSV-1 mutants with lesions in the gK gene but not an HSV-1 with a syn mutation in the gB gene. In addition, there were marked reductions in the plaquing efficiencies and yields of HSV-1 on these cell lines. Cell fusion caused by HSV-1 syn20, a mutant encoding syn gK, was suppressed when cells were coinfected with an Ad vector, AdgK, which expresses wild-type gK. AdgK did not suppress fusion induced by HSV-1 KTTS-1, which expresses syn gB. Conversely, cells coinfected with AdgB, an Ad vector expressing a wild-type form of gB and HSV-1 KTTS.1 (syn gB) were not fused, whereas cells coinfected with AdgB and HSV-1 syn20 (syn gK) were fused. Expression of a number of other HSV-1 glycoproteins using Ad vectors did not reduce membrane fusion induced by syn gK or syn gB. Together, these results support models in which gK and gB participate directly in the fusion of HSV-infected cells. Mutant forms of gB and gK apparently disregulate the fusion process, whereas wild-type forms of gB and gK can act to suppress membrane fusion induced by their mutant counterparts.
Url:
DOI: 10.1006/viro.1993.1507
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<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Herpes Simplex Virus (HSV) Glycoproteins B and K Inhibit Cell Fusion Induced by HSV Syncytial Mutants</title><author><name sortKey="Hutchinson, Lloyd" sort="Hutchinson, Lloyd" uniqKey="Hutchinson L" first="Lloyd" last="Hutchinson">Lloyd Hutchinson</name><affiliation><mods:affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</mods:affiliation></affiliation></author><author><name sortKey="Graham, Frank L" sort="Graham, Frank L" uniqKey="Graham F" first="Frank L." last="Graham">Frank L. Graham</name><affiliation><mods:affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</mods:affiliation></affiliation></author><author><name sortKey="Cai, Weizhong" sort="Cai, Weizhong" uniqKey="Cai W" first="Weizhong" last="Cai">Weizhong Cai</name><affiliation><mods:affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</mods:affiliation></affiliation></author><author><name sortKey="Debroy, Chitrita" sort="Debroy, Chitrita" uniqKey="Debroy C" first="Chitrita" last="Debroy">Chitrita Debroy</name><affiliation><mods:affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</mods:affiliation></affiliation></author><author><name sortKey="Person, Stanley" sort="Person, Stanley" uniqKey="Person S" first="Stanley" last="Person">Stanley Person</name><affiliation><mods:affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</mods:affiliation></affiliation></author><author><name sortKey="Johnson, David C" sort="Johnson, David C" uniqKey="Johnson D" first="David C." last="Johnson">David C. Johnson</name><affiliation><mods:affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:1414D99D91C026B1441B2426262572264777095D</idno><date when="1993" year="1993">1993</date><idno type="doi">10.1006/viro.1993.1507</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-KF0BV07K-9/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">002712</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">002712</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Herpes Simplex Virus (HSV) Glycoproteins B and K Inhibit Cell Fusion Induced by HSV Syncytial Mutants</title><author><name sortKey="Hutchinson, Lloyd" sort="Hutchinson, Lloyd" uniqKey="Hutchinson L" first="Lloyd" last="Hutchinson">Lloyd Hutchinson</name><affiliation><mods:affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</mods:affiliation></affiliation></author><author><name sortKey="Graham, Frank L" sort="Graham, Frank L" uniqKey="Graham F" first="Frank L." last="Graham">Frank L. Graham</name><affiliation><mods:affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</mods:affiliation></affiliation></author><author><name sortKey="Cai, Weizhong" sort="Cai, Weizhong" uniqKey="Cai W" first="Weizhong" last="Cai">Weizhong Cai</name><affiliation><mods:affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</mods:affiliation></affiliation></author><author><name sortKey="Debroy, Chitrita" sort="Debroy, Chitrita" uniqKey="Debroy C" first="Chitrita" last="Debroy">Chitrita Debroy</name><affiliation><mods:affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</mods:affiliation></affiliation></author><author><name sortKey="Person, Stanley" sort="Person, Stanley" uniqKey="Person S" first="Stanley" last="Person">Stanley Person</name><affiliation><mods:affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</mods:affiliation></affiliation></author><author><name sortKey="Johnson, David C" sort="Johnson, David C" uniqKey="Johnson D" first="David C." last="Johnson">David C. Johnson</name><affiliation><mods:affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Virology</title><title level="j" type="abbrev">YVIRO</title><idno type="ISSN">0042-6822</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1993">1993</date><biblScope unit="volume">196</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="514">514</biblScope><biblScope unit="page" to="531">531</biblScope></imprint><idno type="ISSN">0042-6822</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0042-6822</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Herpes simplex virus type 1 (HSV-1) glycoproteins K and B (gK and gB) are intimately involved in virus-induced fusion of cells. Certain mutations in the UL27 (gB) and UL53 (gK) genes confer a syncytial (syn) phenotype characterized by extensive fusion of infected cells and giving rise to multinucleated cells. We have used HSV-1 syn mutants in conjunction with transfected cells or adenovirus vectors to overexpress wild-type gK or gB, in order to study the role of these proteins in virus-induced membrane fusion. Transient expression of wild-type gK inhibited fusion induced by HSV-1 encoding a mutant form of gK (syn gK) but not by viruses encoding a mutant form of gB (syn gB). Stably transformed cells expressing relatively high levels of gK suppressed cell fusion induced by HSV-1 mutants with lesions in the gK gene but not an HSV-1 with a syn mutation in the gB gene. In addition, there were marked reductions in the plaquing efficiencies and yields of HSV-1 on these cell lines. Cell fusion caused by HSV-1 syn20, a mutant encoding syn gK, was suppressed when cells were coinfected with an Ad vector, AdgK, which expresses wild-type gK. AdgK did not suppress fusion induced by HSV-1 KTTS-1, which expresses syn gB. Conversely, cells coinfected with AdgB, an Ad vector expressing a wild-type form of gB and HSV-1 KTTS.1 (syn gB) were not fused, whereas cells coinfected with AdgB and HSV-1 syn20 (syn gK) were fused. Expression of a number of other HSV-1 glycoproteins using Ad vectors did not reduce membrane fusion induced by syn gK or syn gB. Together, these results support models in which gK and gB participate directly in the fusion of HSV-infected cells. Mutant forms of gB and gK apparently disregulate the fusion process, whereas wild-type forms of gB and gK can act to suppress membrane fusion induced by their mutant counterparts.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>Lloyd Hutchinson</name><affiliations><json:string>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</json:string></affiliations></json:item><json:item><name>Frank L. Graham</name><affiliations><json:string>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</json:string></affiliations></json:item><json:item><name>Weizhong Cai</name><affiliations><json:string>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</json:string></affiliations></json:item><json:item><name>Chitrita Debroy</name><affiliations><json:string>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</json:string></affiliations></json:item><json:item><name>Stanley Person</name><affiliations><json:string>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</json:string></affiliations></json:item><json:item><name>David C. Johnson</name><affiliations><json:string>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-KF0BV07K-9</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: Herpes simplex virus type 1 (HSV-1) glycoproteins K and B (gK and gB) are intimately involved in virus-induced fusion of cells. Certain mutations in the UL27 (gB) and UL53 (gK) genes confer a syncytial (syn) phenotype characterized by extensive fusion of infected cells and giving rise to multinucleated cells. We have used HSV-1 syn mutants in conjunction with transfected cells or adenovirus vectors to overexpress wild-type gK or gB, in order to study the role of these proteins in virus-induced membrane fusion. Transient expression of wild-type gK inhibited fusion induced by HSV-1 encoding a mutant form of gK (syn gK) but not by viruses encoding a mutant form of gB (syn gB). Stably transformed cells expressing relatively high levels of gK suppressed cell fusion induced by HSV-1 mutants with lesions in the gK gene but not an HSV-1 with a syn mutation in the gB gene. In addition, there were marked reductions in the plaquing efficiencies and yields of HSV-1 on these cell lines. Cell fusion caused by HSV-1 syn20, a mutant encoding syn gK, was suppressed when cells were coinfected with an Ad vector, AdgK, which expresses wild-type gK. AdgK did not suppress fusion induced by HSV-1 KTTS-1, which expresses syn gB. Conversely, cells coinfected with AdgB, an Ad vector expressing a wild-type form of gB and HSV-1 KTTS.1 (syn gB) were not fused, whereas cells coinfected with AdgB and HSV-1 syn20 (syn gK) were fused. Expression of a number of other HSV-1 glycoproteins using Ad vectors did not reduce membrane fusion induced by syn gK or syn gB. Together, these results support models in which gK and gB participate directly in the fusion of HSV-infected cells. Mutant forms of gB and gK apparently disregulate the fusion process, whereas wild-type forms of gB and gK can act to suppress membrane fusion induced by their mutant counterparts.</abstract><qualityIndicators><score>5.05</score><pdfWordCount>0</pdfWordCount><pdfCharCount>0</pdfCharCount><pdfVersion>1.2</pdfVersion><pdfPageCount>18</pdfPageCount><pdfPageSize>611 x 807 pts</pdfPageSize><refBibsNative>false</refBibsNative><abstractWordCount>308</abstractWordCount><abstractCharCount>1860</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Herpes Simplex Virus (HSV) Glycoproteins B and K Inhibit Cell Fusion Induced by HSV Syncytial Mutants</title><pmid><json:string>8396800</json:string></pmid><pii><json:string>S0042-6822(83)71507-2</json:string></pii><genre><json:string>research-article</json:string></genre><host><title>Virology</title><language><json:string>unknown</json:string></language><publicationDate>1993</publicationDate><issn><json:string>0042-6822</json:string></issn><pii><json:string>S0042-6822(00)X0181-X</json:string></pii><volume>196</volume><issue>2</issue><pages><first>514</first><last>531</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date></date><geogName></geogName><orgName></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName></persName><placeName></placeName><ref_url></ref_url><ref_bibl></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-KF0BV07K-9</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - virology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - virology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Immunology and Microbiology</json:string><json:string>3 - Virology</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string><json:string>4 - vertebres: systeme nerveux et organes des sens</json:string></inist></categories><publicationDate>1993</publicationDate><copyrightDate>1993</copyrightDate><doi><json:string>10.1006/viro.1993.1507</json:string></doi><id>1414D99D91C026B1441B2426262572264777095D</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-KF0BV07K-9/fulltext.pdf</uri></json:item><json:item><extension>ocr</extension><original>false</original><mimetype>text/ocr</mimetype><quality><totalToken>12918</totalToken><correct>10936</correct><rate>79.91328177055377</rate><misspelled>1983</misspelled></quality><langDetect><reliable>true</reliable><languages><json:item><score>955</score><code>en</code><name>ENGLISH</name><percent>99</percent></json:item></languages></langDetect><uri>https://api.istex.fr/ark:/67375/6H6-KF0BV07K-9/fulltext.ocr</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-KF0BV07K-9/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-KF0BV07K-9/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Herpes Simplex Virus (HSV) Glycoproteins B and K Inhibit Cell Fusion Induced by HSV Syncytial Mutants</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>©1993 Academic Press</p></licence><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</p></availability><date>1993</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note><note type="content">Section title: Regular Article</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Herpes Simplex Virus (HSV) Glycoproteins B and K Inhibit Cell Fusion Induced by HSV Syncytial Mutants</title><author xml:id="author-0000"><persName><forename type="first">Lloyd</forename><surname>Hutchinson</surname></persName><affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Frank L.</forename><surname>Graham</surname></persName><affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Weizhong</forename><surname>Cai</surname></persName><affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</affiliation></author><author xml:id="author-0003"><persName><forename type="first">Chitrita</forename><surname>Debroy</surname></persName><affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</affiliation></author><author xml:id="author-0004"><persName><forename type="first">Stanley</forename><surname>Person</surname></persName><affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</affiliation></author><author xml:id="author-0005"><persName><forename type="first">David C.</forename><surname>Johnson</surname></persName><affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</affiliation></author><idno type="istex">1414D99D91C026B1441B2426262572264777095D</idno><idno type="ark">ark:/67375/6H6-KF0BV07K-9</idno><idno type="DOI">10.1006/viro.1993.1507</idno><idno type="PII">S0042-6822(83)71507-2</idno></analytic><monogr><title level="j">Virology</title><title level="j" type="abbrev">YVIRO</title><idno type="pISSN">0042-6822</idno><idno type="PII">S0042-6822(00)X0181-X</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1993"></date><biblScope unit="volume">196</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="514">514</biblScope><biblScope unit="page" to="531">531</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1993</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: Herpes simplex virus type 1 (HSV-1) glycoproteins K and B (gK and gB) are intimately involved in virus-induced fusion of cells. Certain mutations in the UL27 (gB) and UL53 (gK) genes confer a syncytial (syn) phenotype characterized by extensive fusion of infected cells and giving rise to multinucleated cells. We have used HSV-1 syn mutants in conjunction with transfected cells or adenovirus vectors to overexpress wild-type gK or gB, in order to study the role of these proteins in virus-induced membrane fusion. Transient expression of wild-type gK inhibited fusion induced by HSV-1 encoding a mutant form of gK (syn gK) but not by viruses encoding a mutant form of gB (syn gB). Stably transformed cells expressing relatively high levels of gK suppressed cell fusion induced by HSV-1 mutants with lesions in the gK gene but not an HSV-1 with a syn mutation in the gB gene. In addition, there were marked reductions in the plaquing efficiencies and yields of HSV-1 on these cell lines. Cell fusion caused by HSV-1 syn20, a mutant encoding syn gK, was suppressed when cells were coinfected with an Ad vector, AdgK, which expresses wild-type gK. AdgK did not suppress fusion induced by HSV-1 KTTS-1, which expresses syn gB. Conversely, cells coinfected with AdgB, an Ad vector expressing a wild-type form of gB and HSV-1 KTTS.1 (syn gB) were not fused, whereas cells coinfected with AdgB and HSV-1 syn20 (syn gK) were fused. Expression of a number of other HSV-1 glycoproteins using Ad vectors did not reduce membrane fusion induced by syn gK or syn gB. Together, these results support models in which gK and gB participate directly in the fusion of HSV-infected cells. Mutant forms of gB and gK apparently disregulate the fusion process, whereas wild-type forms of gB and gK can act to suppress membrane fusion induced by their mutant counterparts.</p></abstract></profileDesc><revisionDesc><change when="1993">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-KF0BV07K-9/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>YVIRO</jid><aid>71507</aid><ce:pii>S0042-6822(83)71507-2</ce:pii><ce:doi>10.1006/viro.1993.1507</ce:doi><ce:copyright type="full-transfer" year="1993">Academic Press</ce:copyright></item-info><head><ce:dochead><ce:textfn>Regular Article</ce:textfn></ce:dochead><ce:title>Herpes Simplex Virus (HSV) Glycoproteins B and K Inhibit Cell Fusion Induced by HSV Syncytial Mutants</ce:title><ce:author-group><ce:author><ce:given-name>Lloyd</ce:given-name><ce:surname>Hutchinson</ce:surname></ce:author><ce:author><ce:given-name>Frank L.</ce:given-name><ce:surname>Graham</ce:surname></ce:author><ce:author><ce:given-name>Weizhong</ce:given-name><ce:surname>Cai</ce:surname></ce:author><ce:author><ce:given-name>Chitrita</ce:given-name><ce:surname>Debroy</ce:surname></ce:author><ce:author><ce:given-name>Stanley</ce:given-name><ce:surname>Person</ce:surname></ce:author><ce:author><ce:given-name>David C.</ce:given-name><ce:surname>Johnson</ce:surname></ce:author><ce:affiliation><ce:textfn>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</ce:textfn></ce:affiliation></ce:author-group><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Herpes simplex virus type 1 (HSV-1) glycoproteins K and B (gK and gB) are intimately involved in virus-induced fusion of cells. Certain mutations in the UL27 (gB) and UL53 (gK) genes confer a syncytial (syn) phenotype characterized by extensive fusion of infected cells and giving rise to multinucleated cells. We have used HSV-1 syn mutants in conjunction with transfected cells or adenovirus vectors to overexpress wild-type gK or gB, in order to study the role of these proteins in virus-induced membrane fusion. Transient expression of wild-type gK inhibited fusion induced by HSV-1 encoding a mutant form of gK (syn gK) but not by viruses encoding a mutant form of gB (syn gB). Stably transformed cells expressing relatively high levels of gK suppressed cell fusion induced by HSV-1 mutants with lesions in the gK gene but not an HSV-1 with a syn mutation in the gB gene. In addition, there were marked reductions in the plaquing efficiencies and yields of HSV-1 on these cell lines. Cell fusion caused by HSV-1 syn20, a mutant encoding syn gK, was suppressed when cells were coinfected with an Ad vector, AdgK, which expresses wild-type gK. AdgK did not suppress fusion induced by HSV-1 KTTS-1, which expresses syn gB. Conversely, cells coinfected with AdgB, an Ad vector expressing a wild-type form of gB and HSV-1 KTTS.1 (syn gB) were not fused, whereas cells coinfected with AdgB and HSV-1 syn20 (syn gK) were fused. Expression of a number of other HSV-1 glycoproteins using Ad vectors did not reduce membrane fusion induced by syn gK or syn gB. Together, these results support models in which gK and gB participate directly in the fusion of HSV-infected cells. Mutant forms of gB and gK apparently disregulate the fusion process, whereas wild-type forms of gB and gK can act to suppress membrane fusion induced by their mutant counterparts.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Herpes Simplex Virus (HSV) Glycoproteins B and K Inhibit Cell Fusion Induced by HSV Syncytial Mutants</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Herpes Simplex Virus (HSV) Glycoproteins B and K Inhibit Cell Fusion Induced by HSV Syncytial Mutants</title></titleInfo><name type="personal"><namePart type="given">Lloyd</namePart><namePart type="family">Hutchinson</namePart><affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Frank L.</namePart><namePart type="family">Graham</namePart><affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Weizhong</namePart><namePart type="family">Cai</namePart><affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Chitrita</namePart><namePart type="family">Debroy</namePart><affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Stanley</namePart><namePart type="family">Person</namePart><affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">David C.</namePart><namePart type="family">Johnson</namePart><affiliation>Molecular Virology and Immunology Program, Department of Pathology, and Department of Biology, McMaster University, Hamilton, Ontario, Canada, L8N 3Z5; and Department of Molecular and Cell Biology, The Pennsylvania State University, University Park, Pennsylvania 16802</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">1993</dateIssued><copyrightDate encoding="w3cdtf">1993</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Herpes simplex virus type 1 (HSV-1) glycoproteins K and B (gK and gB) are intimately involved in virus-induced fusion of cells. Certain mutations in the UL27 (gB) and UL53 (gK) genes confer a syncytial (syn) phenotype characterized by extensive fusion of infected cells and giving rise to multinucleated cells. We have used HSV-1 syn mutants in conjunction with transfected cells or adenovirus vectors to overexpress wild-type gK or gB, in order to study the role of these proteins in virus-induced membrane fusion. Transient expression of wild-type gK inhibited fusion induced by HSV-1 encoding a mutant form of gK (syn gK) but not by viruses encoding a mutant form of gB (syn gB). Stably transformed cells expressing relatively high levels of gK suppressed cell fusion induced by HSV-1 mutants with lesions in the gK gene but not an HSV-1 with a syn mutation in the gB gene. In addition, there were marked reductions in the plaquing efficiencies and yields of HSV-1 on these cell lines. Cell fusion caused by HSV-1 syn20, a mutant encoding syn gK, was suppressed when cells were coinfected with an Ad vector, AdgK, which expresses wild-type gK. AdgK did not suppress fusion induced by HSV-1 KTTS-1, which expresses syn gB. Conversely, cells coinfected with AdgB, an Ad vector expressing a wild-type form of gB and HSV-1 KTTS.1 (syn gB) were not fused, whereas cells coinfected with AdgB and HSV-1 syn20 (syn gK) were fused. Expression of a number of other HSV-1 glycoproteins using Ad vectors did not reduce membrane fusion induced by syn gK or syn gB. Together, these results support models in which gK and gB participate directly in the fusion of HSV-infected cells. Mutant forms of gB and gK apparently disregulate the fusion process, whereas wild-type forms of gB and gK can act to suppress membrane fusion induced by their mutant counterparts.</abstract><note type="content">Section title: Regular Article</note><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><titleInfo type="abbreviated"><title>YVIRO</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">1993</dateIssued></originInfo><identifier type="ISSN">0042-6822</identifier><identifier type="PII">S0042-6822(00)X0181-X</identifier><part><date>1993</date><detail type="volume"><number>196</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="issue-pages"><start>381</start><end>927</end></extent><extent unit="pages"><start>514</start><end>531</end></extent></part></relatedItem><identifier type="istex">1414D99D91C026B1441B2426262572264777095D</identifier><identifier type="ark">ark:/67375/6H6-KF0BV07K-9</identifier><identifier type="DOI">10.1006/viro.1993.1507</identifier><identifier type="PII">S0042-6822(83)71507-2</identifier><accessCondition type="use and reproduction" contentType="copyright">©1993 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, ©1993</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-KF0BV07K-9/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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