Biosynthesis, structure, and biological activities of envelope protein gp65 of murine coronavirus

Kyoko Yokomori, Nicola La Monica, Shinji Makino, Chien Kou Shieh, Michael M C Lai

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

We have previously shown that gp65 (E3) is a virion structural protein which varies widely in quantity among different strains of mouse hepatitis virus (MHV). In this study, the biosynthetic pathway and possible biological activities of this protein were examined. The glycosylation of gp65 in virus-infected cells was inhibited by tunicamycin but not by monensin, suggesting that it contains an N-glycosidic linkage. Glycosylation is cotranslational and appears to be complete before the glycoprotein reaches the Golgi complex. Pulse-chase experiments showed that this protein decreased in size after 30 min of chase, suggesting that the carbohydrate chains of gp65 undergo trimming during its transport across the Golgi. This interpretation is supported by the endoglycosidase treatment of gp65, which showed that the peptide backbone of gp65 did not decrease in size after pulse-chase periods. This maturation pathway is distinct from that of the E1 or E2 glycoproteins. Partial endoglycosidase treatment indicated that gp65 contains 9 to 10 carbohydrate side chains; thus, almost all of the potential glycosylation sites of gp65 were glycosylated. In vitro translation studies coupled with protease digestion suggest that gp65 is an integral membrane protein. The presence of gp65 in the virion is correlated with the presence of an acetylesterase activity. No hemagglutinin activity was detected.

Original languageEnglish (US)
Pages (from-to)683-691
Number of pages9
JournalVirology
Volume173
Issue number2
DOIs
StatePublished - 1989
Externally publishedYes

Fingerprint

Coronavirus
Glycosylation
Glycoside Hydrolases
Virion
Glycoproteins
Carbohydrates
Acetylesterase
Murine hepatitis virus
Tunicamycin
Monensin
Proteins
Biosynthetic Pathways
Hemagglutinins
Golgi Apparatus
Digestion
Membrane Proteins
Peptide Hydrolases
Viruses
Peptides

ASJC Scopus subject areas

  • Virology
  • Infectious Diseases

Cite this

Biosynthesis, structure, and biological activities of envelope protein gp65 of murine coronavirus. / Yokomori, Kyoko; La Monica, Nicola; Makino, Shinji; Shieh, Chien Kou; Lai, Michael M C.

In: Virology, Vol. 173, No. 2, 1989, p. 683-691.

Research output: Contribution to journalArticle

Yokomori, Kyoko ; La Monica, Nicola ; Makino, Shinji ; Shieh, Chien Kou ; Lai, Michael M C. / Biosynthesis, structure, and biological activities of envelope protein gp65 of murine coronavirus. In: Virology. 1989 ; Vol. 173, No. 2. pp. 683-691.
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