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 Callebaut, P. E. Articles by Pensaert, M. B. Search for Related Content PubMed PubMed Citation Articles by Callebaut, P. E. Articles by Pensaert, M. B. Agricola Articles by Callebaut, P. E. Articles by Pensaert, M. B.

Characterization and Isolation of Structural Polypeptides in Haemagglutinating Encephalomyelitis Virus

Laboratory of Virology, Faculty of Veterinary Medicine, University of Gent, Casinoplein 24, B-9000 Gent, Belgium

Haemagglutinating encephalomyelitis virus (HEV), a member of the coronavirus family, was purified and analysed by SDS-polyacrylamide gel electrophoresis. It was shown to contain eight polypeptides, seven of which were glycosylated. They had apparent mol. wt. of 180000 (GP 180), 130000 (GP 130), 120000 (GP 120) 76000 (GP 76), 64000 (VP 64), 54000 (GP 54), 32000 (GP 32) and 31000 (GP 31). Electrophoresis of virus samples dissociated under varying conditions showed that GP 54 and GP 120 could be interpreted as larger products of GP 31 and GP 32 and of GP 76, respectively. GP 76 also appeared as a dimer with a mol. wt. of 140000 (GP 140) in the absence of -mercaptoethanol. Subviral particles, obtained by treatment with bromelain, banded at a slightly lower density than the intact virus and lacked surface projections. Analysis of these particles indicated that GP 180, GP 130 and GP 76 are associated with the virus projections. A small part of GP 31 and GP 32 also appeared to protrude from the lipid envelope, since 20% of each molecule was sensitive to digestion. Two glycoproteins, GP 130 and GP 76, were solubilized with the detergent Triton X-100 and separated by rate zonal centrifugation. According to its activity in indirect haemagglutination tests, GP 76 was considered to be a monovalent haemagglutinin subunit.

Received 11 October 1979; accepted 1 January 1980.

This article has been cited by other articles:

				A. Lissenberg, M. M. Vrolijk, A. L. W. van Vliet, M. A. Langereis, J. D. F. de Groot-Mijnes, P. J. M. Rottier, and R. J. de Groot Luxury at a Cost? Recombinant Mouse Hepatitis Viruses Expressing the Accessory Hemagglutinin Esterase Protein Display Reduced Fitness In Vitro J. Virol., December 15, 2005; 79(24): 15054 - 15063. [Abstract] [Full Text] [PDF]