Isolation of Subviral Components from Transmissible Gastroenteritis Virus

Microbiology Department, Institute for Research on Animal Diseases, Agricultural Research Council, Compton, Newbury, Berkshire, RG16 0NN, U.K. Exposure of purified transmissible gastroenteritis virus, a porcine coronavirus, to non-ionic detergents resulted in the removal of the surface projections a...

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Bibliographic Details
Published in:Journal of general virology 1976-08, Vol.32 (2), p.283-294
Main Authors: Garwes, D. J, Pocock, D. H, Pike, Brenda V
Format: Article
Language:English
Subjects:
Arginine - analysis
Coronaviridae - analysis
Glycopeptides - analysis
Glycoproteins - isolation & purification
Lipids - analysis
Lipids - isolation & purification
Peptides - analysis
Phospholipids - analysis
RNA, Viral - analysis
Sulfates - analysis
Surface-Active Agents - pharmacology
Transmissible gastroenteritis virus - analysis
Transmissible gastroenteritis virus - ultrastructure
Viral Proteins - analysis
Viral Proteins - isolation & purification
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Summary:Microbiology Department, Institute for Research on Animal Diseases, Agricultural Research Council, Compton, Newbury, Berkshire, RG16 0NN, U.K. Exposure of purified transmissible gastroenteritis virus, a porcine coronavirus, to non-ionic detergents resulted in the removal of the surface projections and > 98% of the virus lipid. Virus RNA was associated with a subviral particle which had a sedimentation coefficient of 650S, compared with 495S for the intact virion, and which banded in Cs 2 SO 4 gradients at 1.295 g/ml. Negatively stained preparations of subviral particles were shown by electron microscopy to contain spherical particles of 60 to 70 nm diam., similar in appearance to those derived from oncornaviruses. Polyacrylamide gel electrophoresis of the polypeptides from isolated subviral particles showed that these structures contained three of the four major virus structural proteins, the arginine-rich polypeptide VP2 and the two membrane glycopolypeptides VP3 and 4. The detergent-liberated surface projections, composed of a single species of sulphated glycopolypeptide, VP1, were isolated by rate-zonal centrifugation through sucrose gradients followed by precipitation with ammonium sulphate in the presence of bovine serum albumin. Received 12 February 1976; accepted 1 April 1976.
ISSN:0022-1317
1465-2099
DOI:10.1099/0022-1317-32-2-283