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

Identifieur interne : 000069 ( PascalFrancis/Curation ); précédent : 000068; suivant : 000070

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

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

Source :

RBID : Pascal:98-0511618

Descripteurs français

English descriptors

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.
pA  
A01 01  1    @0 0304-8608
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
A60       @1 P
A61       @0 A
A64   1    @0 Archives of virology
A66 01      @0 AUT
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
C03 01  X  FRE  @0 Virus hépatite murine @2 NW @5 01
C03 01  X  ENG  @0 Murine hepatitis virus @2 NW @5 01
C03 01  X  SPA  @0 Murine hepatitis virus @2 NW @5 01
C03 02  X  FRE  @0 Hémagglutinine @5 04
C03 02  X  ENG  @0 Hemagglutinin @5 04
C03 02  X  SPA  @0 Hemoaglutinina @5 04
C03 03  X  FRE  @0 Esterases @2 FE @5 05
C03 03  X  ENG  @0 Esterases @2 FE @5 05
C03 03  X  SPA  @0 Esterases @2 FE @5 05
C03 04  X  FRE  @0 Caractérisation @5 06
C03 04  X  ENG  @0 Characterization @5 06
C03 04  X  SPA  @0 Caracterización @5 06
C03 05  X  FRE  @0 Activité enzymatique @5 07
C03 05  X  ENG  @0 Enzymatic activity @5 07
C03 05  X  SPA  @0 Actividad enzimática @5 07
C03 06  X  FRE  @0 Spécificité substrat @5 08
C03 06  X  ENG  @0 Substrate specificity @5 08
C03 06  X  SPA  @0 Especificidad sustrato @5 08
C07 01  X  FRE  @0 Coronavirus @2 NW
C07 01  X  ENG  @0 Coronavirus @2 NW
C07 01  X  SPA  @0 Coronavirus @2 NW
C07 02  X  FRE  @0 Coronaviridae @2 NW
C07 02  X  ENG  @0 Coronaviridae @2 NW
C07 02  X  SPA  @0 Coronaviridae @2 NW
C07 03  X  FRE  @0 Nidovirales @2 NW
C07 03  X  ENG  @0 Nidovirales @2 NW
C07 03  X  SPA  @0 Nidovirales @2 NW
C07 04  X  FRE  @0 Virus @2 NW
C07 04  X  ENG  @0 Virus @2 NW
C07 04  X  SPA  @0 Virus @2 NW
C07 05  X  FRE  @0 Hydrolases @2 FE
C07 05  X  ENG  @0 Hydrolases @2 FE
C07 05  X  SPA  @0 Hydrolases @2 FE
C07 06  X  FRE  @0 Enzyme
C07 06  X  ENG  @0 Enzyme
C07 06  X  SPA  @0 Enzima
C07 07  X  FRE  @0 Relation hôte virus @5 43
C07 07  X  ENG  @0 Host virus relation @5 43
C07 07  X  SPA  @0 Relación huesped virus @5 43
N21       @1 334

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Pascal:98-0511618

Le document en format XML

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<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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<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>NW</s2>
</fC07>
<fC07 i1="03" i2="X" l="ENG">
<s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="03" i2="X" l="SPA">
<s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="04" i2="X" l="FRE">
<s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="04" i2="X" l="ENG">
<s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="04" i2="X" l="SPA">
<s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="05" i2="X" l="FRE">
<s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="05" i2="X" l="ENG">
<s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="05" i2="X" l="SPA">
<s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="06" i2="X" l="FRE">
<s0>Enzyme</s0>
</fC07>
<fC07 i1="06" i2="X" l="ENG">
<s0>Enzyme</s0>
</fC07>
<fC07 i1="06" i2="X" l="SPA">
<s0>Enzima</s0>
</fC07>
<fC07 i1="07" i2="X" l="FRE">
<s0>Relation hôte virus</s0>
<s5>43</s5>
</fC07>
<fC07 i1="07" i2="X" l="ENG">
<s0>Host virus relation</s0>
<s5>43</s5>
</fC07>
<fC07 i1="07" i2="X" l="SPA">
<s0>Relación huesped virus</s0>
<s5>43</s5>
</fC07>
<fN21>
<s1>334</s1>
</fN21>
</pA>
</standard>
</inist>
</record>

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