Haemagglutinin-esterase protein (HE) of murine corona virus: DVIMD (diarrhea virus of infant mice)
Identifieur interne : 001692 ( Ncbi/Merge ); précédent : 001691; suivant : 001693Haemagglutinin-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.
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 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
PubMed: 9739331
PubMed Central: 7086961
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PMC:7086961Le document en format XML
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<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>
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<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>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Coronavirus</term>
</keywords>
<keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Acetylesterase</term>
<term>Hémagglutinines virales</term>
<term>Protéines virales</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Hémagglutinines virales</term>
<term>Protéines virales</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Hemagglutinins, Viral</term>
<term>Viral Proteins</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Female</term>
<term>Mice</term>
<term>Mice, Inbred BALB C</term>
<term>Substrate Specificity</term>
<term>Viral Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Femelle</term>
<term>Protéines de fusion virale</term>
<term>Souris</term>
<term>Souris de lignée BALB C</term>
<term>Spécificité du substrat</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<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>
</front>
</TEI>
</pubmed>
</double>
</record>
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