Haemagglutinating encephalomyelitis virus (HEV), a member of the coronavirus group, was adapted for growth in adult pig thyroid cell cultures and purified by ammonium sulphate precipitation and rate zonal centrifugation through sucrose gradients. Polyacrylamide gel electrophoresis of samples of purified virus revealed the presence of five polypeptides, four of which contained carbohydrate. The molecular weights of these proteins were 180000 (gp 180), 125000 (gp 125), 100000 (gp 100), 56000 (p 56) and 26 500 (gp 26.5). After treatment of the virus with the non-ionic detergent Nonidet P40, two subviral components were isolated. As RNA-containing particle, sedimenting in sucrose gradients at the same rate as untreated virus, was analysed and found to contain two polypeptides, p 56 and gp 26.5. The second complex sedimented at a much slower rate and contained three glycoproteins gp 180, gp 125 and gp 100. Comparison of these findings with data published for other members of the coronavirus group is discussed.


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