Haemagglutinin-esterase protein (HE) of murine corona virus: DVIM (diarrhea virus of infant mice).
Identifieur interne : 000D82 ( PubMed/Corpus ); précédent : 000D81; suivant : 000D83Haemagglutinin-esterase protein (HE) of murine corona virus: DVIM (diarrhea virus of infant mice).
Auteurs : K. Sugiyama ; M. Kasai ; S. Kato ; H. Kasai ; K. HatakeyamaSource :
- Archives of virology [ 0304-8608 ] ; 1998.
English descriptors
- KwdEn :
- Acetylesterase (analysis), Acetylesterase (isolation & purification), Animals, Coronavirus (enzymology), Female, Hemagglutinins, Viral (analysis), Hemagglutinins, Viral (isolation & purification), Hemagglutinins, Viral (physiology), Mice, Mice, Inbred BALB C, Substrate Specificity, Viral Fusion Proteins, Viral Proteins (analysis), Viral Proteins (isolation & purification), Viral Proteins (physiology).
- MESH :
- chemical , analysis : Acetylesterase, Hemagglutinins, Viral, Viral Proteins.
- chemical , isolation & purification : Acetylesterase, Hemagglutinins, Viral, Viral Proteins.
- enzymology : Coronavirus.
- chemical , physiology : Hemagglutinins, Viral, Viral Proteins.
- Animals, Female, Mice, Mice, Inbred BALB C, Substrate Specificity, Viral Fusion Proteins.
Abstract
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 alpha-naphthylacetate (alpha-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 alpha-NA in vitro. MHV-S reacted efficiently with both p-NiA and alpha-NA but less with BSM. Influenza virus (C/Miyagi/77) reacted with BSM efficiently, however reacted with p-NiA weakly, but not with alpha-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.
DOI: 10.1007/s007050050395
PubMed: 9739331
Links to Exploration step
pubmed:9739331Le document en format XML
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<author><name sortKey="Sugiyama, K" sort="Sugiyama, K" uniqKey="Sugiyama K" first="K" last="Sugiyama">K. Sugiyama</name>
<affiliation><nlm:affiliation>Department of Biology, Faculty of Science, Hirosaki University, Japan.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Kasai, M" sort="Kasai, M" uniqKey="Kasai M" first="M" last="Kasai">M. Kasai</name>
</author>
<author><name sortKey="Kato, S" sort="Kato, S" uniqKey="Kato S" first="S" last="Kato">S. Kato</name>
</author>
<author><name sortKey="Kasai, H" sort="Kasai, H" uniqKey="Kasai H" first="H" last="Kasai">H. Kasai</name>
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<author><name sortKey="Hatakeyama, K" sort="Hatakeyama, K" uniqKey="Hatakeyama K" first="K" last="Hatakeyama">K. Hatakeyama</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Haemagglutinin-esterase protein (HE) of murine corona virus: DVIM (diarrhea virus of infant mice).</title>
<author><name sortKey="Sugiyama, K" sort="Sugiyama, K" uniqKey="Sugiyama K" first="K" last="Sugiyama">K. Sugiyama</name>
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<series><title level="j">Archives of virology</title>
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<term>Coronavirus (enzymology)</term>
<term>Female</term>
<term>Hemagglutinins, Viral (analysis)</term>
<term>Hemagglutinins, Viral (isolation & purification)</term>
<term>Hemagglutinins, Viral (physiology)</term>
<term>Mice</term>
<term>Mice, Inbred BALB C</term>
<term>Substrate Specificity</term>
<term>Viral Fusion Proteins</term>
<term>Viral Proteins (analysis)</term>
<term>Viral Proteins (isolation & purification)</term>
<term>Viral Proteins (physiology)</term>
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<keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Acetylesterase</term>
<term>Hemagglutinins, Viral</term>
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<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Acetylesterase</term>
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<term>Viral Proteins</term>
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<term>Female</term>
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<front><div type="abstract" xml:lang="en">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 alpha-naphthylacetate (alpha-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 alpha-NA in vitro. MHV-S reacted efficiently with both p-NiA and alpha-NA but less with BSM. Influenza virus (C/Miyagi/77) reacted with BSM efficiently, however reacted with p-NiA weakly, but not with alpha-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>
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<Title>Archives of virology</Title>
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<ArticleTitle>Haemagglutinin-esterase protein (HE) of murine corona virus: DVIM (diarrhea virus of infant mice).</ArticleTitle>
<Pagination><MedlinePgn>1523-34</MedlinePgn>
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<Abstract><AbstractText>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 alpha-naphthylacetate (alpha-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 alpha-NA in vitro. MHV-S reacted efficiently with both p-NiA and alpha-NA but less with BSM. Influenza virus (C/Miyagi/77) reacted with BSM efficiently, however reacted with p-NiA weakly, but not with alpha-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.</AbstractText>
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