CovidV1, PubMed, Curation, bibRecord, 000728

Haemagglutinin-esterase protein (HE) of murine corona virus: DVIM (diarrhea virus of infant mice).

Identifieur interne : 000728 ( PubMed/Curation ); précédent : 000727; suivant : 000729

Haemagglutinin-esterase protein (HE) of murine corona virus: DVIM (diarrhea virus of infant mice).

Auteurs : K. Sugiyama [Japon] ; M. Kasai ; S. Kato ; H. Kasai ; K. Hatakeyama

Source :

Archives of virology [ 0304-8608 ] ; 1998.

RBID : pubmed:9739331

Descripteurs français

KwdFr :
- Acetylesterase (analyse), Acetylesterase (isolement et purification), Animaux, Coronavirus (enzymologie), Femelle, Hémagglutinines virales (analyse), Hémagglutinines virales (isolement et purification), Hémagglutinines virales (physiologie), Protéines de fusion virale, Protéines virales (analyse), Protéines virales (isolement et purification), Protéines virales (physiologie), Souris, Souris de lignée BALB C, Spécificité du substrat.
MESH :
- analyse : Acetylesterase, Hémagglutinines virales, Protéines virales.
- enzymologie : Coronavirus.
- isolement et purification : Acetylesterase, Hémagglutinines virales, Protéines virales.
- physiologie : Hémagglutinines virales, Protéines virales.
- Animaux, Femelle, Protéines de fusion virale, Souris, Souris de lignée BALB C, Spécificité du substrat.

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

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Le document en format XML

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<affiliation wicri:level="1"><nlm:affiliation>Department of Biology, Faculty of Science, Hirosaki University, Japan.</nlm:affiliation>
<country xml:lang="fr">Japon</country>
<wicri:regionArea>Department of Biology, Faculty of Science, Hirosaki University</wicri:regionArea>
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<author><name sortKey="Kasai, M" sort="Kasai, M" uniqKey="Kasai M" first="M" last="Kasai">M. Kasai</name>
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<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>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Acetylesterase (analyse)</term>
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<term>Coronavirus (enzymologie)</term>
<term>Femelle</term>
<term>Hémagglutinines virales (analyse)</term>
<term>Hémagglutinines virales (isolement et purification)</term>
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<term>Souris de lignée BALB C</term>
<term>Spécificité du substrat</term>
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<term>Hemagglutinins, Viral</term>
<term>Viral Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Acetylesterase</term>
<term>Hemagglutinins, Viral</term>
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<term>Substrate Specificity</term>
<term>Viral Fusion Proteins</term>
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<term>Femelle</term>
<term>Protéines de fusion virale</term>
<term>Souris</term>
<term>Souris de lignée BALB C</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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<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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Haemagglutinin-esterase protein (HE) of murine corona virus: DVIM (diarrhea virus of infant mice).

Haemagglutinin-esterase protein (HE) of murine corona virus: DVIM (diarrhea virus of infant mice).

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki