SUMMARYHaemagglutinating 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 tool. wt. of 180000 (GP T8o), I3OOOO (GP T3o), I2oooo (GP tzo) 760oo (GP 76), 64ooo (VP 64), 54ooo (GP 54), 32000 (GP 32) and 3I ooo (GP 31). Electrophoresis of virus samples dissociated under varying conditions showed that GP 54 and GP I2O could be interpreted as larger products of GP 3I and GP 32 and of GP 76, respectively. GP 76 also appeared as a dimer with a mol. wt. of 14o00o (GP t4o) in the absence of fl-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 I8o, GP I3o 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 2o % of each molecule was sensitive to digestion. Two glycoproteins, GP i 30 and GP 76, were solubilized with the detergent Triton X-Ioo and separated by rate zonal centrifugation. According to its activity in indirect haemagglutination tests, GP 76 was considered to be a monovalent haemagglutinin subunit.