Haemagglutinin-esterase protein (HE) of murine corona virus: DVIMD (diarrhea virus of infant mice)
Identifieur interne : 000285 ( Istex/Curation ); précédent : 000284; suivant : 000286Haemagglutinin-esterase protein (HE) of murine corona virus: DVIMD (diarrhea virus of infant mice)
Auteurs : K. Sugiyama [Japon] ; M. Kasai [Japon] ; S. Kato [Japon] ; H. Kasai [Japon] ; K. Hatakeyama [Japon]Source :
- 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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Sugiyama</name><affiliation wicri:level="1"><mods:affiliation>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan, Japan</mods:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan</wicri:regionArea></affiliation></author><author><name sortKey="Kasai, M" sort="Kasai, M" uniqKey="Kasai M" first="M." last="Kasai">M. Kasai</name><affiliation wicri:level="1"><mods:affiliation>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan, Japan</mods:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan</wicri:regionArea></affiliation></author><author><name sortKey="Kato, S" sort="Kato, S" uniqKey="Kato S" first="S." last="Kato">S. 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Hatakeyama</name><affiliation wicri:level="1"><mods:affiliation>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan, Japan</mods:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan</wicri:regionArea></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></record>Pour manipuler ce document sous Unix (Dilib)
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