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I Vvtts Research, 5 (1986) 131-144 Elsevier VRR 00262 Structural proteins of human respiratory coronavirus OC43 Brenda G. Hogue and David A. Brian Department of MitroAtology'. The Umuerslty of Tennessee, Knoscd/e. ITV J7996-0RJ5, L'.S.A. (Accepted for publication 28 February 1986) Summary 131 The human respiratory coronavirus OC43 was grown on a human rectal tumor cell line and was isotopically labeled with amino acids, glucosamine. and orthophos- phate to analyze virion structural proteins. Four major protein species were resolved by efectrophoresis and many of their properties were deduced from digestion studies using proteolytic enzymes. The four proteins are: (1) A 190 kDa protein, the presumed peplomeric protein. that was glycosylated and proteolytically cleavable by trypsin into subunits of 110 and 90 kDa. The subunits each represent a different amino acid sequence on the basis of peptide mapping: (2) a 130 kDa protein that was glycosylated and behaved as a disulfide-linked dimer of 65 kDa molecules. It is the apparent virion hemagglutinin on the basis of digestion studies with trypsin, bromelain and pronase: (3) a 55 kDa nucleocapsid protein that was phosphorylated: (4) a 26 kDa matrix protein that was glycosylated. The 190, 130, 55 and 26 kDa species can therefore be designated P. H, N and M, respectively. They exist in molar ratios of 4: 1: 33 : 33, and are calculated to be present at the rate of 88, 22, 726, and 726 molecules per virion, respectively. human respiratory coronovirus OC43, structural proteins Introduction Coronaviruses are estimated to cause approximately 20 'C of upper respiratory disease in humans (Larsen ct al., 1980; McIntosh et al., 1970). Human respiratorv coronaviruses are found as either one of two antigenic types: those related to human coronavirus OC43 (viruses that could originally he grown only in tracheal organ culture), and those related to human coronavirus 229E (viruses that could be 0168-1702/86/503.50 ~- t986 Elsevier Science Publishers B.N '. (Biornedical Di, u1 o. D