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. 1998;17(2):123–128. doi: 10.1023/A:1008060522426

Primary Structures of Hemagglutinin-esterase and Spike Glycoproteins of Murine Coronavirus DVIM

Eiji Morita 1, Hirotaka Ebina 1, Akira Muto 1, Hyouta Himeno 1, Koki Hatakeyama 1, Kazuo Sugiyama 1,
PMCID: PMC7089163  PMID: 9857985

Abstract

Diarrhea virus of infant mice (DVIM) is a member of murine hepatitis viruses (MHVs). The nucleotide sequences of the genes encoding the hemagglutinin-esterase (HE) and the spike (S) glycoproteins from DVIM were determined and compared with those of other MHVs. The deduced amino acid sequence of the HE protein was most similar to that of MHV-S strain (94% identity), and the S protein sequence was most similar to that of MHV-Y strain (90% identity). The DVIM HE protein has a unique N-linked glycosylation site in addition to other glycosylation sites common to many MHV strains. Unlike in some typical MHV strain, such as MHV-A59 and MHV-JHM, the vast majority of the S glycoprotein molecules in DVIM exist an uncleaved form probably due to several amino acid substitutions around the cleavage site.

Keywords: MHV, DVIM, hemagglutinin-esterase glycoprotein, spike glycoprotein, cleavage of surface glycoprotein, N-linked glycosylation site

References


Articles from Virus Genes are provided here courtesy of Nature Publishing Group

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