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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Haemagglutinin-esterase protein (HE) of murine corona virus: DVIMD (diarrhea virus of infant mice)</title>
<author><name sortKey="Sugiyama, K" sort="Sugiyama, K" uniqKey="Sugiyama K" first="K." last="Sugiyama">K. Sugiyama</name>
<affiliation><nlm:aff id="Aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kasai, M" sort="Kasai, M" uniqKey="Kasai M" first="M." last="Kasai">M. Kasai</name>
<affiliation><nlm:aff id="Aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kato, S" sort="Kato, S" uniqKey="Kato S" first="S." last="Kato">S. Kato</name>
<affiliation><nlm:aff id="Aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kasai, H" sort="Kasai, H" uniqKey="Kasai H" first="H." last="Kasai">H. Kasai</name>
<affiliation><nlm:aff id="Aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Hatakeyama, K" sort="Hatakeyama, K" uniqKey="Hatakeyama K" first="K." last="Hatakeyama">K. Hatakeyama</name>
<affiliation><nlm:aff id="Aff1"></nlm:aff>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PMC</idno>
<idno type="pmid">9739331</idno>
<idno type="pmc">7086961</idno>
<idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7086961</idno>
<idno type="RBID">PMC:7086961</idno>
<idno type="doi">10.1007/s007050050395</idno>
<date when="1998">1998</date>
<idno type="wicri:Area/Pmc/Corpus">000187</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000187</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Haemagglutinin-esterase protein (HE) of murine corona virus: DVIMD (diarrhea virus of infant mice)</title>
<author><name sortKey="Sugiyama, K" sort="Sugiyama, K" uniqKey="Sugiyama K" first="K." last="Sugiyama">K. Sugiyama</name>
<affiliation><nlm:aff id="Aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kasai, M" sort="Kasai, M" uniqKey="Kasai M" first="M." last="Kasai">M. Kasai</name>
<affiliation><nlm:aff id="Aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kato, S" sort="Kato, S" uniqKey="Kato S" first="S." last="Kato">S. Kato</name>
<affiliation><nlm:aff id="Aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kasai, H" sort="Kasai, H" uniqKey="Kasai H" first="H." last="Kasai">H. Kasai</name>
<affiliation><nlm:aff id="Aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Hatakeyama, K" sort="Hatakeyama, K" uniqKey="Hatakeyama K" first="K." last="Hatakeyama">K. Hatakeyama</name>
<affiliation><nlm:aff id="Aff1"></nlm:aff>
</affiliation>
</author>
</analytic>
<series><title level="j">Archives of Virology</title>
<idno type="ISSN">0304-8608</idno>
<idno type="eISSN">1432-8798</idno>
<imprint><date when="1998">1998</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass></textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><title>Summary</title>
<p>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>
</div>
</front>
</TEI>
<pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Arch Virol</journal-id>
<journal-id journal-id-type="iso-abbrev">Arch. Virol</journal-id>
<journal-title-group><journal-title>Archives of Virology</journal-title>
</journal-title-group>
<issn pub-type="ppub">0304-8608</issn>
<issn pub-type="epub">1432-8798</issn>
<publisher><publisher-name>Springer-Verlag</publisher-name>
<publisher-loc>Vienna</publisher-loc>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">9739331</article-id>
<article-id pub-id-type="pmc">7086961</article-id>
<article-id pub-id-type="publisher-id">81431523</article-id>
<article-id pub-id-type="doi">10.1007/s007050050395</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Article</subject>
</subj-group>
</article-categories>
<title-group><article-title>Haemagglutinin-esterase protein (HE) of murine corona virus: DVIMD (diarrhea virus of infant mice)</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Sugiyama</surname>
<given-names>K.</given-names>
</name>
<xref ref-type="aff" rid="Aff1"></xref>
</contrib>
<contrib contrib-type="author"><name><surname>Kasai</surname>
<given-names>M.</given-names>
</name>
<xref ref-type="aff" rid="Aff1"></xref>
</contrib>
<contrib contrib-type="author"><name><surname>Kato</surname>
<given-names>S.</given-names>
</name>
<xref ref-type="aff" rid="Aff1"></xref>
</contrib>
<contrib contrib-type="author"><name><surname>Kasai</surname>
<given-names>H.</given-names>
</name>
<xref ref-type="aff" rid="Aff1"></xref>
</contrib>
<contrib contrib-type="author"><name><surname>Hatakeyama</surname>
<given-names>K.</given-names>
</name>
<xref ref-type="aff" rid="Aff1"></xref>
</contrib>
<aff id="Aff1"><institution-wrap><institution-id institution-id-type="GRID">grid.257016.7</institution-id>
<institution-id institution-id-type="ISNI">0000000106736172</institution-id>
<institution>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan,</institution>
</institution-wrap>
Japan</aff>
</contrib-group>
<pub-date pub-type="epub"><day>7</day>
<month>4</month>
<year>2014</year>
</pub-date>
<pub-date pub-type="ppub"><year>1998</year>
</pub-date>
<volume>143</volume>
<issue>8</issue>
<fpage>1523</fpage>
<lpage>1534</lpage>
<permissions><copyright-statement>© Springer-Verlag 1998</copyright-statement>
<license><license-p>This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.</license-p>
</license>
</permissions>
<abstract id="Abs1"><title>Summary</title>
<p>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>
<custom-meta-group><custom-meta><meta-name>issue-copyright-statement</meta-name>
<meta-value>© Springer-Verlag 1998</meta-value>
</custom-meta>
</custom-meta-group>
</article-meta>
</front>
<back><fn-group><fn><p>Accepted March 24, 1998</p>
</fn>
</fn-group>
</back>
</pmc>
</record>
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