CovidV1, PascalFrancis, Checkpoint, bibRecord, 000059

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

Identifieur interne : 000059 ( PascalFrancis/Checkpoint ); précédent : 000058; suivant : 000060

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 :

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.

Affiliations:

Japon

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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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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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