CovidV1, PascalFrancis, Corpus, bibRecord, 000061

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

Identifieur interne : 000061 ( PascalFrancis/Corpus ); précédent : 000060; suivant : 000062

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

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

Source :

Archives of virology [ 0304-8608 ] ; 1998.

RBID : Pascal:98-0511618

Descripteurs français

Pascal (Inist)
- Virus hépatite murine, Hémagglutinine, Esterases, Caractérisation, Activité enzymatique, Spécificité substrat.

English descriptors

KwdEn :
- Characterization, Enzymatic activity, Esterases, Hemagglutinin, Murine hepatitis virus, Substrate specificity.

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.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

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A03		`1`		`@0 Arch. virol.`
A05				`@2 143`
A06				`@2 8`
A08	`01`	`1`	`ENG`	`@1 Haemagglutinin-esterase protein (HE) of murine corona virus : DVIM (diarrhea virus of infant mice)`
A11	`01`	`1`		`@1 SUGIYAMA (K.)`
A11	`02`	`1`		`@1 KASAI (M.)`
A11	`03`	`1`		`@1 KATO (S.)`
A11	`04`	`1`		`@1 KASAI (H.)`
A11	`05`	`1`		`@1 HATAKEYAMA (K.)`
A14	`01`			`@1 Department of Biology, Faculty of Science, Hirosaki University @2 Hirosaki @3 JPN @Z 1 aut. @Z 2 aut. @Z 3 aut. @Z 4 aut. @Z 5 aut.`
A20				`@1 1523-1534`
A21				`@1 1998`
A23	`01`			`@0 ENG`
A43	`01`			`@1 INIST @2 6355 @5 354000070929690060`
A44				`@0 0000 @1 © 1998 INIST-CNRS. All rights reserved.`
A45				`@0 33 ref.`
A47	`01`	`1`		`@0 98-0511618`
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A64		`1`		`@0 Archives of virology`
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C01	`01`		`ENG`	@0 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.
C02	`01`	`X`		`@0 002A05C03`
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C03	`01`	`X`	`ENG`	`@0 Murine hepatitis virus @2 NW @5 01`
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C03	`02`	`X`	`FRE`	`@0 Hémagglutinine @5 04`
C03	`02`	`X`	`ENG`	`@0 Hemagglutinin @5 04`
C03	`02`	`X`	`SPA`	`@0 Hemoaglutinina @5 04`
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C03	`06`	`X`	`SPA`	`@0 Especificidad sustrato @5 08`
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C07	`02`	`X`	`FRE`	`@0 Coronaviridae @2 NW`
C07	`02`	`X`	`ENG`	`@0 Coronaviridae @2 NW`
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C07	`03`	`X`	`SPA`	`@0 Nidovirales @2 NW`
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N21				`@1 334`

Format Inist (serveur)

NO :	PASCAL 98-0511618 INIST
ET :	Haemagglutinin-esterase protein (HE) of murine corona virus : DVIM (diarrhea virus of infant mice)
AU :	SUGIYAMA (K.); KASAI (M.); KATO (S.); KASAI (H.); HATAKEYAMA (K.)
AF :	Department of Biology, Faculty of Science, Hirosaki University/Hirosaki/Japon (1 aut., 2 aut., 3 aut., 4 aut., 5 aut.)
DT :	Publication en série; Niveau analytique
SO :	Archives of virology; ISSN 0304-8608; Autriche; Da. 1998; Vol. 143; No. 8; Pp. 1523-1534; Bibl. 33 ref.
LA :	Anglais
EA :	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.
CC :	002A05C03
FD :	Virus hépatite murine; Hémagglutinine; Esterases; Caractérisation; Activité enzymatique; Spécificité substrat
FG :	Coronavirus; Coronaviridae; Nidovirales; Virus; Hydrolases; Enzyme; Relation hôte virus
ED :	Murine hepatitis virus; Hemagglutinin; Esterases; Characterization; Enzymatic activity; Substrate specificity
EG :	Coronavirus; Coronaviridae; Nidovirales; Virus; Hydrolases; Enzyme; Host virus relation
SD :	Murine hepatitis virus; Hemoaglutinina; Esterases; Caracterización; Actividad enzimática; Especificidad sustrato
LO :	INIST-6355.354000070929690060
ID :	98-0511618

Links to Exploration step

Pascal:98-0511618

Le document en format XML

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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 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>
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<fC01 i1="01" l="ENG"><s0>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.</s0>
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<s2>FE</s2>
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<s2>FE</s2>
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<fC07 i1="06" i2="X" l="ENG"><s0>Enzyme</s0>
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<fC07 i1="06" i2="X" l="SPA"><s0>Enzima</s0>
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<fC07 i1="07" i2="X" l="FRE"><s0>Relation hôte virus</s0>
<s5>43</s5>
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<fC07 i1="07" i2="X" l="ENG"><s0>Host virus relation</s0>
<s5>43</s5>
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<fC07 i1="07" i2="X" l="SPA"><s0>Relación huesped virus</s0>
<s5>43</s5>
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<fN21><s1>334</s1>
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<server><NO>PASCAL 98-0511618 INIST</NO>
<ET>Haemagglutinin-esterase protein (HE) of murine corona virus : DVIM (diarrhea virus of infant mice)</ET>
<AU>SUGIYAMA (K.); KASAI (M.); KATO (S.); KASAI (H.); HATAKEYAMA (K.)</AU>
<AF>Department of Biology, Faculty of Science, Hirosaki University/Hirosaki/Japon (1 aut., 2 aut., 3 aut., 4 aut., 5 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Archives of virology; ISSN 0304-8608; Autriche; Da. 1998; Vol. 143; No. 8; Pp. 1523-1534; Bibl. 33 ref.</SO>
<LA>Anglais</LA>
<EA>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.</EA>
<CC>002A05C03</CC>
<FD>Virus hépatite murine; Hémagglutinine; Esterases; Caractérisation; Activité enzymatique; Spécificité substrat</FD>
<FG>Coronavirus; Coronaviridae; Nidovirales; Virus; Hydrolases; Enzyme; Relation hôte virus</FG>
<ED>Murine hepatitis virus; Hemagglutinin; Esterases; Characterization; Enzymatic activity; Substrate specificity</ED>
<EG>Coronavirus; Coronaviridae; Nidovirales; Virus; Hydrolases; Enzyme; Host virus relation</EG>
<SD>Murine hepatitis virus; Hemoaglutinina; Esterases; Caracterización; Actividad enzimática; Especificidad sustrato</SD>
<LO>INIST-6355.354000070929690060</LO>
<ID>98-0511618</ID>
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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)

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