HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Deregt, D. Articles by Babiuk, L. A. Search for Related Content PubMed PubMed Citation Articles by Deregt, D. Articles by Babiuk, L. A. Agricola Articles by Deregt, D. Articles by Babiuk, L. A.

Structural Proteins of Bovine Coronavirus and Their Intracellular Processing

¹ Veterinary Microbiology, University of Saskatchewan
and the² Veterinary Infectious Disease Organization, 124 Veterinary Road, Saskatoon, Saskatchewan, Canada, S7N 0W0

The Quebec isolate of bovine coronavirus (BCV) was found to contain four unique major structural proteins. These proteins consisted of the peplomeric protein (gp190/E2, gp100/E2), the nucleocapsid protein (p53/N) and its apparent trimer (p160/N), a family of small matrix glycoproteins (gp26/E1, gp25/E1 and p23/E1) and the putative haemagglutinin (gp124/E3). Pulse-chase experiments utilizing polyclonal antiserum and monoclonal antibodies indicated that the unique BCV E3 protein had as its primary precursor an N-linked glycoprotein with an M_r of 59000 (gp59) which underwent rapid dimerization by disulphide bond formation to yield gp118. Further glycosylation of gp118 produced gp124/E3 which incorporated fucose. Thus gp124/E3 was probably a homodimer. The processing of the E2 and E1 proteins of BCV was similar to that shown previously for mouse hepatitis virus. A large N-linked precursor glycoprotein, gp170, underwent further glycosylation to yield gp190/E2 before subsequent proteolytic cleavage to yield gp100/E2. The glycosylated E1 (gp26, gp25) proteins arose as a result of O-linked glycosylation of p23/E1 as indicated by the resistance of these species to tunicamycin.

Keywords: bovine coronavirus, structural proteins, glycoprotein processing

Received 13 April 1987; accepted 14 July 1987.

This article has been cited by other articles:

				X.Q. LIN, V.N. CHOULJENKO, K.G. KOUSOULAS, and J. STORZ Temperature-sensitive acetylesterase activity of haemagglutinin-esterase specified by respiratory bovine coronaviruses J. Med. Microbiol., December 1, 2000; 49(12): 1119 - 1127. [Abstract] [Full Text] [PDF]

				C. A. M. de Haan, P. Roestenberg, M. de Wit, A. A. F. de Vries, T. Nilsson, H. Vennema, and P. J. M. Rottier Structural Requirements for O-Glycosylation of the Mouse Hepatitis Virus Membrane Protein J. Biol. Chem., November 6, 1998; 273(45): 29905 - 29914. [Abstract] [Full Text] [PDF]