Membrane and Phospholipid Binding by Murine Coronaviral Nucleocapsid N Protein
Identifieur interne : 000240 ( Istex/Corpus ); précédent : 000239; suivant : 000241Membrane and Phospholipid Binding by Murine Coronaviral Nucleocapsid N Protein
Auteurs : Robert Anderson ; Fred WongSource :
- Virology [ 0042-6822 ] ; 1993.
Abstract
Abstract: Evidence is presented which indicates that membrane binding of the murine coronavirus, mouse hepatitis virus (MHV) nucleocapsid (N) protein is mediated by certain lipids. Binding of N protein to membranes of mouse fibroblast L-2 cells is very specific and occurs under conditions in which no other viral or cellular proteins show datectable binding. Binding occurs with both free and nucleocapsid-associated N protein, arguing for membrane-binding sites on the N protein itself, rather than on RNA. Binding of N protein also occurs to membranes in the absence of MHV matrix (M) protein which is known to interact with the N protein. Both non-viral, single-stranded RNA and DNA inhibit membrane binding of N protein. In addition, purified phospholipid liposomes compete against N protein binding to membranes. Of various phospholipids tested, cardiolipin was the most effective in inhibiting membrane binding. The N protein was also shown to bind directly to phospholipid liposomes containing cardiolipin as well as to liposomes containing total lipids extracted from mouse L-2 cells. Because of certain structural similarities between phospholipids and nucleic acids, we speculate that membrane lipid association of the N protein may compete for RNA binding sites on the N protein. Such a mechanism may be important for processes such as nucleocapsid uncoating and nucleocapsid assembly. Most interestingly the properties of phospholipid and nucleic acid binding are markedly similar to those recently described for the bacterial DNA-binding proteins DnaA and recA.
Url:
DOI: 10.1006/viro.1993.1253
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<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Membrane and Phospholipid Binding by Murine Coronaviral Nucleocapsid N Protein</title><author><name sortKey="Anderson, Robert" sort="Anderson, Robert" uniqKey="Anderson R" first="Robert" last="Anderson">Robert Anderson</name><affiliation><mods:affiliation>Department of Microbiology and Infectious Diseases, Faculty of Medicine, University of Calgary, Calgary, Alberta T2N 4N1, Canada</mods:affiliation></affiliation></author><author><name sortKey="Wong, Fred" sort="Wong, Fred" uniqKey="Wong F" first="Fred" last="Wong">Fred Wong</name><affiliation><mods:affiliation>Department of Microbiology and Infectious Diseases, Faculty of Medicine, University of Calgary, Calgary, Alberta T2N 4N1, Canada</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:79C9AAAC18877260C0C911FFF9A39DAEFA746950</idno><date when="1993" year="1993">1993</date><idno type="doi">10.1006/viro.1993.1253</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-BZQB7SML-3/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000240</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000240</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Membrane and Phospholipid Binding by Murine Coronaviral Nucleocapsid N Protein</title><author><name sortKey="Anderson, Robert" sort="Anderson, Robert" uniqKey="Anderson R" first="Robert" last="Anderson">Robert Anderson</name><affiliation><mods:affiliation>Department of Microbiology and Infectious Diseases, Faculty of Medicine, University of Calgary, Calgary, Alberta T2N 4N1, Canada</mods:affiliation></affiliation></author><author><name sortKey="Wong, Fred" sort="Wong, Fred" uniqKey="Wong F" first="Fred" last="Wong">Fred Wong</name><affiliation><mods:affiliation>Department of Microbiology and Infectious Diseases, Faculty of Medicine, University of Calgary, Calgary, Alberta T2N 4N1, Canada</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">194</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="224">224</biblScope><biblScope unit="page" to="232">232</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: Evidence is presented which indicates that membrane binding of the murine coronavirus, mouse hepatitis virus (MHV) nucleocapsid (N) protein is mediated by certain lipids. Binding of N protein to membranes of mouse fibroblast L-2 cells is very specific and occurs under conditions in which no other viral or cellular proteins show datectable binding. Binding occurs with both free and nucleocapsid-associated N protein, arguing for membrane-binding sites on the N protein itself, rather than on RNA. Binding of N protein also occurs to membranes in the absence of MHV matrix (M) protein which is known to interact with the N protein. Both non-viral, single-stranded RNA and DNA inhibit membrane binding of N protein. In addition, purified phospholipid liposomes compete against N protein binding to membranes. Of various phospholipids tested, cardiolipin was the most effective in inhibiting membrane binding. The N protein was also shown to bind directly to phospholipid liposomes containing cardiolipin as well as to liposomes containing total lipids extracted from mouse L-2 cells. Because of certain structural similarities between phospholipids and nucleic acids, we speculate that membrane lipid association of the N protein may compete for RNA binding sites on the N protein. Such a mechanism may be important for processes such as nucleocapsid uncoating and nucleocapsid assembly. Most interestingly the properties of phospholipid and nucleic acid binding are markedly similar to those recently described for the bacterial DNA-binding proteins DnaA and recA.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>Robert Anderson</name><affiliations><json:string>Department of Microbiology and Infectious Diseases, Faculty of Medicine, University of Calgary, Calgary, Alberta T2N 4N1, Canada</json:string></affiliations></json:item><json:item><name>Fred Wong</name><affiliations><json:string>Department of Microbiology and Infectious Diseases, Faculty of Medicine, University of Calgary, Calgary, Alberta T2N 4N1, Canada</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-BZQB7SML-3</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: Evidence is presented which indicates that membrane binding of the murine coronavirus, mouse hepatitis virus (MHV) nucleocapsid (N) protein is mediated by certain lipids. Binding of N protein to membranes of mouse fibroblast L-2 cells is very specific and occurs under conditions in which no other viral or cellular proteins show datectable binding. Binding occurs with both free and nucleocapsid-associated N protein, arguing for membrane-binding sites on the N protein itself, rather than on RNA. Binding of N protein also occurs to membranes in the absence of MHV matrix (M) protein which is known to interact with the N protein. Both non-viral, single-stranded RNA and DNA inhibit membrane binding of N protein. In addition, purified phospholipid liposomes compete against N protein binding to membranes. Of various phospholipids tested, cardiolipin was the most effective in inhibiting membrane binding. The N protein was also shown to bind directly to phospholipid liposomes containing cardiolipin as well as to liposomes containing total lipids extracted from mouse L-2 cells. Because of certain structural similarities between phospholipids and nucleic acids, we speculate that membrane lipid association of the N protein may compete for RNA binding sites on the N protein. Such a mechanism may be important for processes such as nucleocapsid uncoating and nucleocapsid assembly. 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Binding of N protein to membranes of mouse fibroblast L-2 cells is very specific and occurs under conditions in which no other viral or cellular proteins show datectable binding. Binding occurs with both free and nucleocapsid-associated N protein, arguing for membrane-binding sites on the N protein itself, rather than on RNA. Binding of N protein also occurs to membranes in the absence of MHV matrix (M) protein which is known to interact with the N protein. Both non-viral, single-stranded RNA and DNA inhibit membrane binding of N protein. In addition, purified phospholipid liposomes compete against N protein binding to membranes. Of various phospholipids tested, cardiolipin was the most effective in inhibiting membrane binding. The N protein was also shown to bind directly to phospholipid liposomes containing cardiolipin as well as to liposomes containing total lipids extracted from mouse L-2 cells. Because of certain structural similarities between phospholipids and nucleic acids, we speculate that membrane lipid association of the N protein may compete for RNA binding sites on the N protein. Such a mechanism may be important for processes such as nucleocapsid uncoating and nucleocapsid assembly. Most interestingly the properties of phospholipid and nucleic acid binding are markedly similar to those recently described for the bacterial DNA-binding proteins DnaA and recA.</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-BZQB7SML-3/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>71253</aid><ce:pii>S0042-6822(83)71253-5</ce:pii><ce:doi>10.1006/viro.1993.1253</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>Membrane and Phospholipid Binding by Murine Coronaviral Nucleocapsid N Protein</ce:title><ce:author-group><ce:author><ce:given-name>Robert</ce:given-name><ce:surname>Anderson</ce:surname></ce:author><ce:author><ce:given-name>Fred</ce:given-name><ce:surname>Wong</ce:surname></ce:author><ce:affiliation><ce:textfn>Department of Microbiology and Infectious Diseases, Faculty of Medicine, University of Calgary, Calgary, Alberta T2N 4N1, Canada</ce:textfn></ce:affiliation></ce:author-group><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Evidence is presented which indicates that membrane binding of the murine coronavirus, mouse hepatitis virus (MHV) nucleocapsid (N) protein is mediated by certain lipids. Binding of N protein to membranes of mouse fibroblast L-2 cells is very specific and occurs under conditions in which no other viral or cellular proteins show datectable binding. Binding occurs with both free and nucleocapsid-associated N protein, arguing for membrane-binding sites on the N protein itself, rather than on RNA. Binding of N protein also occurs to membranes in the absence of MHV matrix (M) protein which is known to interact with the N protein. Both non-viral, single-stranded RNA and DNA inhibit membrane binding of N protein. In addition, purified phospholipid liposomes compete against N protein binding to membranes. Of various phospholipids tested, cardiolipin was the most effective in inhibiting membrane binding. The N protein was also shown to bind directly to phospholipid liposomes containing cardiolipin as well as to liposomes containing total lipids extracted from mouse L-2 cells. Because of certain structural similarities between phospholipids and nucleic acids, we speculate that membrane lipid association of the N protein may compete for RNA binding sites on the N protein. Such a mechanism may be important for processes such as nucleocapsid uncoating and nucleocapsid assembly. Most interestingly the properties of phospholipid and nucleic acid binding are markedly similar to those recently described for the bacterial DNA-binding proteins DnaA and recA.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Membrane and Phospholipid Binding by Murine Coronaviral Nucleocapsid N Protein</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Membrane and Phospholipid Binding by Murine Coronaviral Nucleocapsid N Protein</title></titleInfo><name type="personal"><namePart type="given">Robert</namePart><namePart type="family">Anderson</namePart><affiliation>Department of Microbiology and Infectious Diseases, Faculty of Medicine, University of Calgary, Calgary, Alberta T2N 4N1, Canada</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Fred</namePart><namePart type="family">Wong</namePart><affiliation>Department of Microbiology and Infectious Diseases, Faculty of Medicine, University of Calgary, Calgary, Alberta T2N 4N1, Canada</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: Evidence is presented which indicates that membrane binding of the murine coronavirus, mouse hepatitis virus (MHV) nucleocapsid (N) protein is mediated by certain lipids. Binding of N protein to membranes of mouse fibroblast L-2 cells is very specific and occurs under conditions in which no other viral or cellular proteins show datectable binding. Binding occurs with both free and nucleocapsid-associated N protein, arguing for membrane-binding sites on the N protein itself, rather than on RNA. Binding of N protein also occurs to membranes in the absence of MHV matrix (M) protein which is known to interact with the N protein. Both non-viral, single-stranded RNA and DNA inhibit membrane binding of N protein. In addition, purified phospholipid liposomes compete against N protein binding to membranes. Of various phospholipids tested, cardiolipin was the most effective in inhibiting membrane binding. The N protein was also shown to bind directly to phospholipid liposomes containing cardiolipin as well as to liposomes containing total lipids extracted from mouse L-2 cells. Because of certain structural similarities between phospholipids and nucleic acids, we speculate that membrane lipid association of the N protein may compete for RNA binding sites on the N protein. Such a mechanism may be important for processes such as nucleocapsid uncoating and nucleocapsid assembly. Most interestingly the properties of phospholipid and nucleic acid binding are markedly similar to those recently described for the bacterial DNA-binding proteins DnaA and recA.</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)X0177-8</identifier><part><date>1993</date><detail type="volume"><number>194</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>432</end></extent><extent unit="pages"><start>224</start><end>232</end></extent></part></relatedItem><identifier type="istex">79C9AAAC18877260C0C911FFF9A39DAEFA746950</identifier><identifier type="ark">ark:/67375/6H6-BZQB7SML-3</identifier><identifier type="DOI">10.1006/viro.1993.1253</identifier><identifier type="PII">S0042-6822(83)71253-5</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-BZQB7SML-3/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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