Antigenic and polypeptide structure of bovine enteric coronavirus as defined by monoclonal antibodies.

Abstract

Bovine enteric coronavirus (BECV), characterized by Stair et al (1972), is now recognized as one of the viral agents that cause acute diarrhoea in young calves (Stair et al, 1972). Virions are large and pleomorphic (100 to 150 nm in diameter) and possess a fringe of characteristically club-shaped peplomers, 20 nm long (Sharpee et al, 1976). Polypeptide analysis revealed 3 major proteins including glycoproteins of high (GP 65/125 — 65,000 and 125,000 daltons in molecular weight) and low (GP25) molecular weight and a phosphorylated protein (VP 50) (King and Brian, 1982; Laporte and Bobulesco, 1981). Two minor glycoproteins have also been described, GP 105 and GP 100 (King and Brian, 1982; J. Laporte, personal communication). Detergent treatment and limited proteolysis of purified virions enabled to localize the structural proteins (King and Brian, 1982; Bobulesco, 1983). The peplomers are mainly constituted of GP 125, a glycoprotein which is reduced to a GP 65 component by 2-Mercaptoethanol (2-ME), and of GP 105 and GP 100. On these outer projections are located the structural sites responsible for haemagglutination and virus to cell interactions. GP 25 is more deeply embedded in the virion envelope and interacts with the internal nucleoprotein (Bobulesco, 1983). VP 50 is an internal phosphoprotein, closely associated with the viral genome (King and Brian, 1982).KeywordsHaemagglutination AssayCytosol ExtractFeline Infectious PeritonitisFeline Infectious Peritonitis VirusMurine Hepatitis VirusThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.