Haemagglutinin-esterase protein (HE) of murine corona virus: DVIMD (diarrhea virus of infant mice)
Identifieur interne : 000305 ( Istex/Corpus ); précédent : 000304; suivant : 000306Haemagglutinin-esterase protein (HE) of murine corona virus: DVIMD (diarrhea virus of infant mice)
Auteurs : K. Sugiyama ; M. Kasai ; S. Kato ; H. Kasai ; K. HatakeyamaSource :
- Archives of Virology [ 0304-8608 ] ; 1998-07-01.
Abstract
Summary: The acetylesterase (AE) activity of DVIM (diarrhea virus of infant mice) was assigned to the haemagglutinin-esterase (HE) protein. The substrate specificity was examined using the natural substrate bovine submaxillary mucin (BSM) and/or synthetic substrates p-nitrophenylacetate (p-NiA) and α-naphthylacetate (α-NA) and compared with several strains of MHV and influenza viruses. The AE of DVIM hydrolyzed the O-acetylester bond of BSM, and the two synthetic substrates p-NiA and α-NA in vitro. MHV-S reacted efficiently with both p-NiA and α-NA but less with BSM. Influenza virus (C/Miyagi/77) reacted with BSM efficiently, however reacted with p-NiA weakly, but not with α-NA at all. Thus, the AE-reactivity of DVIM was distinctly different from that of MHV-S and influenza C virus, suggesting that the AE of HE may have a modified function. Isolation of HE by the treatment with non ionic detergent NP40, resulted in globules approximately 5 nm in diameter. DVIM-binding proteins were demonstrated in the plasma membrane of mouse intestinal brush-border cells and hepatocytes. The same protein was recognized by MHV-S and MHV-4. The cell membranes obtained from these target tissues were substrates for the AE of DVIM. The biological importance of the HE protein for DVIM is discussed.
Url:
DOI: 10.1007/s007050050395
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Kato</name><affiliation><mods:affiliation>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan, Japan</mods:affiliation></affiliation></author><author><name sortKey="Kasai, H" sort="Kasai, H" uniqKey="Kasai H" first="H." last="Kasai">H. Kasai</name><affiliation><mods:affiliation>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan, Japan</mods:affiliation></affiliation></author><author><name sortKey="Hatakeyama, K" sort="Hatakeyama, K" uniqKey="Hatakeyama K" first="K." last="Hatakeyama">K. 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Sugiyama</name><affiliation><mods:affiliation>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan, Japan</mods:affiliation></affiliation></author><author><name sortKey="Kasai, M" sort="Kasai, M" uniqKey="Kasai M" first="M." last="Kasai">M. Kasai</name><affiliation><mods:affiliation>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan, Japan</mods:affiliation></affiliation></author><author><name sortKey="Kato, S" sort="Kato, S" uniqKey="Kato S" first="S." last="Kato">S. Kato</name><affiliation><mods:affiliation>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan, Japan</mods:affiliation></affiliation></author><author><name sortKey="Kasai, H" sort="Kasai, H" uniqKey="Kasai H" first="H." last="Kasai">H. Kasai</name><affiliation><mods:affiliation>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan, Japan</mods:affiliation></affiliation></author><author><name sortKey="Hatakeyama, K" sort="Hatakeyama, K" uniqKey="Hatakeyama K" first="K." last="Hatakeyama">K. Hatakeyama</name><affiliation><mods:affiliation>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan, Japan</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Archives of Virology</title><title level="j" type="abbrev">Arch. Virol.</title><idno type="ISSN">0304-8608</idno><idno type="eISSN">1432-8798</idno><imprint><publisher>Springer-Verlag</publisher><pubPlace>Vienna</pubPlace><date type="published" when="1998-07-01">1998-07-01</date><biblScope unit="volume">143</biblScope><biblScope unit="issue">8</biblScope><biblScope unit="page" from="1523">1523</biblScope><biblScope unit="page" to="1534">1534</biblScope></imprint><idno type="ISSN">0304-8608</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0304-8608</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Summary: The acetylesterase (AE) activity of DVIM (diarrhea virus of infant mice) was assigned to the haemagglutinin-esterase (HE) protein. The substrate specificity was examined using the natural substrate bovine submaxillary mucin (BSM) and/or synthetic substrates p-nitrophenylacetate (p-NiA) and α-naphthylacetate (α-NA) and compared with several strains of MHV and influenza viruses. The AE of DVIM hydrolyzed the O-acetylester bond of BSM, and the two synthetic substrates p-NiA and α-NA in vitro. MHV-S reacted efficiently with both p-NiA and α-NA but less with BSM. Influenza virus (C/Miyagi/77) reacted with BSM efficiently, however reacted with p-NiA weakly, but not with α-NA at all. Thus, the AE-reactivity of DVIM was distinctly different from that of MHV-S and influenza C virus, suggesting that the AE of HE may have a modified function. Isolation of HE by the treatment with non ionic detergent NP40, resulted in globules approximately 5 nm in diameter. DVIM-binding proteins were demonstrated in the plasma membrane of mouse intestinal brush-border cells and hepatocytes. The same protein was recognized by MHV-S and MHV-4. The cell membranes obtained from these target tissues were substrates for the AE of DVIM. The biological importance of the HE protein for DVIM is discussed.</div></front></TEI><istex><corpusName>springer-journals</corpusName><author><json:item><name>K. Sugiyama</name><affiliations><json:string>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan, Japan</json:string></affiliations></json:item><json:item><name>M. Kasai</name><affiliations><json:string>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan, Japan</json:string></affiliations></json:item><json:item><name>S. Kato</name><affiliations><json:string>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan, Japan</json:string></affiliations></json:item><json:item><name>H. 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The substrate specificity was examined using the natural substrate bovine submaxillary mucin (BSM) and/or synthetic substrates p-nitrophenylacetate (p-NiA) and α-naphthylacetate (α-NA) and compared with several strains of MHV and influenza viruses. The AE of DVIM hydrolyzed the O-acetylester bond of BSM, and the two synthetic substrates p-NiA and α-NA in vitro. MHV-S reacted efficiently with both p-NiA and α-NA but less with BSM. Influenza virus (C/Miyagi/77) reacted with BSM efficiently, however reacted with p-NiA weakly, but not with α-NA at all. Thus, the AE-reactivity of DVIM was distinctly different from that of MHV-S and influenza C virus, suggesting that the AE of HE may have a modified function. Isolation of HE by the treatment with non ionic detergent NP40, resulted in globules approximately 5 nm in diameter. DVIM-binding proteins were demonstrated in the plasma membrane of mouse intestinal brush-border cells and hepatocytes. The same protein was recognized by MHV-S and MHV-4. The cell membranes obtained from these target tissues were substrates for the AE of DVIM. 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Virol.</title><idno type="pISSN">0304-8608</idno><idno type="eISSN">1432-8798</idno><idno type="journal-ID">true</idno><idno type="issue-article-count">17</idno><idno type="volume-issue-count">12</idno><imprint><publisher>Springer-Verlag</publisher><pubPlace>Vienna</pubPlace><date type="published" when="1998-07-01"></date><biblScope unit="volume">143</biblScope><biblScope unit="issue">8</biblScope><biblScope unit="page" from="1523">1523</biblScope><biblScope unit="page" to="1534">1534</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1998</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Summary: The acetylesterase (AE) activity of DVIM (diarrhea virus of infant mice) was assigned to the haemagglutinin-esterase (HE) protein. The substrate specificity was examined using the natural substrate bovine submaxillary mucin (BSM) and/or synthetic substrates p-nitrophenylacetate (p-NiA) and α-naphthylacetate (α-NA) and compared with several strains of MHV and influenza viruses. The AE of DVIM hydrolyzed the O-acetylester bond of BSM, and the two synthetic substrates p-NiA and α-NA in vitro. MHV-S reacted efficiently with both p-NiA and α-NA but less with BSM. Influenza virus (C/Miyagi/77) reacted with BSM efficiently, however reacted with p-NiA weakly, but not with α-NA at all. Thus, the AE-reactivity of DVIM was distinctly different from that of MHV-S and influenza C virus, suggesting that the AE of HE may have a modified function. Isolation of HE by the treatment with non ionic detergent NP40, resulted in globules approximately 5 nm in diameter. DVIM-binding proteins were demonstrated in the plasma membrane of mouse intestinal brush-border cells and hepatocytes. The same protein was recognized by MHV-S and MHV-4. The cell membranes obtained from these target tissues were substrates for the AE of DVIM. The biological importance of the HE protein for DVIM is discussed.</p></abstract><textClass><keywords scheme="Journal-Subject-Group"><list><label>SCB</label><item><term>Biomedicine</term></item><label>SCB22003</label><item><term>Virology</term></item><label>SCB16003</label><item><term>Medical Microbiology</term></item><label>SCH33096</label><item><term>Infectious Diseases</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1998-07-01">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/VQC-CR9M0C0V-V/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="corpus springer-journals not found" wicri:toSee="no header"><istex:xmlDeclaration>version="1.0" encoding="UTF-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//Springer-Verlag//DTD A++ V2.4//EN" URI="http://devel.springer.de/A++/V2.4/DTD/A++V2.4.dtd" name="istex:docType"></istex:docType><istex:document><Publisher><PublisherInfo><PublisherName>Springer-Verlag</PublisherName><PublisherLocation>Vienna</PublisherLocation></PublisherInfo><Journal><JournalInfo JournalProductType="ArchiveJournal" NumberingStyle="Unnumbered"><JournalID>705</JournalID><JournalPrintISSN>0304-8608</JournalPrintISSN><JournalElectronicISSN>1432-8798</JournalElectronicISSN><JournalTitle>Archives of Virology</JournalTitle><JournalAbbreviatedTitle>Arch. Virol.</JournalAbbreviatedTitle><JournalSubjectGroup><JournalSubject Code="SCB" Type="Primary">Biomedicine</JournalSubject><JournalSubject Code="SCB22003" Priority="1" Type="Secondary">Virology</JournalSubject><JournalSubject Code="SCB16003" Priority="2" Type="Secondary">Medical Microbiology</JournalSubject><JournalSubject Code="SCH33096" Priority="3" Type="Secondary">Infectious Diseases</JournalSubject></JournalSubjectGroup></JournalInfo><Volume><VolumeInfo TocLevels="0" VolumeType="Regular"><VolumeIDStart>143</VolumeIDStart><VolumeIDEnd>143</VolumeIDEnd><VolumeIssueCount>12</VolumeIssueCount></VolumeInfo><Issue IssueType="Regular"><IssueInfo TocLevels="0"><IssueIDStart>8</IssueIDStart><IssueIDEnd>8</IssueIDEnd><IssueArticleCount>17</IssueArticleCount><IssueHistory><CoverDate><Year>1998</Year><Month>7</Month></CoverDate></IssueHistory><IssueCopyright><CopyrightHolderName>Springer-Verlag</CopyrightHolderName><CopyrightYear>1998</CopyrightYear></IssueCopyright></IssueInfo><Article ID="Art6"><ArticleInfo ArticleType="OriginalPaper" ContainsESM="No" Language="En" NumberingStyle="Unnumbered" TocLevels="0"><ArticleID>81431523</ArticleID><ArticleDOI>10.1007/s007050050395</ArticleDOI><ArticleSequenceNumber>6</ArticleSequenceNumber><ArticleTitle Language="En">Haemagglutinin-esterase protein (HE) of murine corona virus: DVIMD (diarrhea virus of infant mice)</ArticleTitle><ArticleFirstPage>1523</ArticleFirstPage><ArticleLastPage>1534</ArticleLastPage><ArticleHistory><RegistrationDate><Year>1998</Year><Month>4</Month><Day>7</Day></RegistrationDate><OnlineDate><Year>2014</Year><Month>4</Month><Day>7</Day></OnlineDate></ArticleHistory><ArticleCopyright><CopyrightHolderName>Springer-Verlag</CopyrightHolderName><CopyrightYear>1998</CopyrightYear></ArticleCopyright><ArticleGrants Type="Regular"><MetadataGrant Grant="OpenAccess"></MetadataGrant><AbstractGrant Grant="OpenAccess"></AbstractGrant><BodyPDFGrant Grant="Restricted"></BodyPDFGrant><BodyHTMLGrant Grant="Restricted"></BodyHTMLGrant><BibliographyGrant Grant="Restricted"></BibliographyGrant><ESMGrant Grant="Restricted"></ESMGrant></ArticleGrants></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>K.</GivenName><FamilyName>Sugiyama</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>M.</GivenName><FamilyName>Kasai</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>S.</GivenName><FamilyName>Kato</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>H.</GivenName><FamilyName>Kasai</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>K.</GivenName><FamilyName>Hatakeyama</FamilyName></AuthorName></Author><Affiliation ID="Aff1"><OrgName>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan</OrgName><OrgAddress><Country>Japan</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Summary</Heading><Para>The acetylesterase (AE) activity of DVIM (diarrhea virus of infant mice) was assigned to the haemagglutinin-esterase (HE) protein. The substrate specificity was examined using the natural substrate bovine submaxillary mucin (BSM) and/or synthetic substrates p-nitrophenylacetate (p-NiA) and α-naphthylacetate (α-NA) and compared with several strains of MHV and influenza viruses. The AE of DVIM hydrolyzed the O-acetylester bond of BSM, and the two synthetic substrates p-NiA and α-NA in vitro. MHV-S reacted efficiently with both p-NiA and α-NA but less with BSM. Influenza virus (C/Miyagi/77) reacted with BSM efficiently, however reacted with p-NiA weakly, but not with α-NA at all. Thus, the AE-reactivity of DVIM was distinctly different from that of MHV-S and influenza C virus, suggesting that the AE of HE may have a modified function. Isolation of HE by the treatment with non ionic detergent NP40, resulted in globules approximately 5 nm in diameter. DVIM-binding proteins were demonstrated in the plasma membrane of mouse intestinal brush-border cells and hepatocytes. The same protein was recognized by MHV-S and MHV-4. The cell membranes obtained from these target tissues were substrates for the AE of DVIM. The biological importance of the HE protein for DVIM is discussed.</Para></Abstract><ArticleNote Type="Misc"><SimplePara>Accepted March 24, 1998</SimplePara></ArticleNote></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Haemagglutinin-esterase protein (HE) of murine corona virus: DVIMD (diarrhea virus of infant mice)</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Haemagglutinin-esterase protein (HE) of murine corona virus: DVIMD (diarrhea virus of infant mice)</title></titleInfo><name type="personal"><namePart type="given">K.</namePart><namePart type="family">Sugiyama</namePart><affiliation>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M.</namePart><namePart type="family">Kasai</namePart><affiliation>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">S.</namePart><namePart type="family">Kato</namePart><affiliation>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">H.</namePart><namePart type="family">Kasai</namePart><affiliation>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">K.</namePart><namePart type="family">Hatakeyama</namePart><affiliation>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="OriginalPaper" 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>Springer-Verlag</publisher><place><placeTerm type="text">Vienna</placeTerm></place><dateIssued encoding="w3cdtf">1998-07-01</dateIssued><copyrightDate encoding="w3cdtf">1998</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Summary: The acetylesterase (AE) activity of DVIM (diarrhea virus of infant mice) was assigned to the haemagglutinin-esterase (HE) protein. The substrate specificity was examined using the natural substrate bovine submaxillary mucin (BSM) and/or synthetic substrates p-nitrophenylacetate (p-NiA) and α-naphthylacetate (α-NA) and compared with several strains of MHV and influenza viruses. The AE of DVIM hydrolyzed the O-acetylester bond of BSM, and the two synthetic substrates p-NiA and α-NA in vitro. MHV-S reacted efficiently with both p-NiA and α-NA but less with BSM. Influenza virus (C/Miyagi/77) reacted with BSM efficiently, however reacted with p-NiA weakly, but not with α-NA at all. Thus, the AE-reactivity of DVIM was distinctly different from that of MHV-S and influenza C virus, suggesting that the AE of HE may have a modified function. Isolation of HE by the treatment with non ionic detergent NP40, resulted in globules approximately 5 nm in diameter. DVIM-binding proteins were demonstrated in the plasma membrane of mouse intestinal brush-border cells and hepatocytes. The same protein was recognized by MHV-S and MHV-4. The cell membranes obtained from these target tissues were substrates for the AE of DVIM. The biological importance of the HE protein for DVIM is discussed.</abstract><relatedItem type="host"><titleInfo><title>Archives of Virology</title></titleInfo><titleInfo type="abbreviated"><title>Arch. Virol.</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>Springer</publisher><dateIssued encoding="w3cdtf">1998-07-01</dateIssued><copyrightDate encoding="w3cdtf">1998</copyrightDate></originInfo><subject><genre>Journal-Subject-Group</genre><topic authority="SpringerSubjectCodes" authorityURI="SCB">Biomedicine</topic><topic authority="SpringerSubjectCodes" authorityURI="SCB22003">Virology</topic><topic authority="SpringerSubjectCodes" authorityURI="SCB16003">Medical Microbiology</topic><topic authority="SpringerSubjectCodes" authorityURI="SCH33096">Infectious Diseases</topic></subject><identifier type="ISSN">0304-8608</identifier><identifier type="eISSN">1432-8798</identifier><identifier type="JournalID">705</identifier><identifier type="IssueArticleCount">17</identifier><identifier type="VolumeIssueCount">12</identifier><part><date>1998</date><detail type="volume"><number>143</number><caption>vol.</caption></detail><detail type="issue"><number>8</number><caption>no.</caption></detail><extent unit="pages"><start>1523</start><end>1534</end></extent></part><recordInfo><recordOrigin>Springer-Verlag, 1998</recordOrigin></recordInfo></relatedItem><identifier type="istex">8FCC5CAFB0AE66AF9BBB6F375D73A434555BE1DB</identifier><identifier type="ark">ark:/67375/VQC-CR9M0C0V-V</identifier><identifier type="DOI">10.1007/s007050050395</identifier><identifier type="ArticleID">81431523</identifier><identifier type="ArticleID">Art6</identifier><accessCondition type="use and reproduction" contentType="copyright">Springer-Verlag, 1998</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-3XSW68JL-F">springer</recordContentSource><recordOrigin>Springer-Verlag, 1998</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-CR9M0C0V-V/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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