Characterization of Glycoprotein Complexes Present in Human Cytomegalovirus Envelopes

Abstract

Summary Three disulphide cross-bridged glycoprotein complexes were immunoprecipitated from purified human cytomegalovirus envelopes using a monoclonal antibody with a specificity for a glycoprotein of mol. wt. 52 × 103. These complexes were isolated by electroelution after polyacrylamide gel electrophoresis (PAGE) under non-reducing conditions. Compositional analysis of each complex by PAGE under reducing conditions showed that at least two distinct complexes,one containing glycoproteins with mol. wt. of 52 × 103 and 95 × 103 and the other with glycoproteins of 52 × 103 and 130 × 103, were present. The results obtained indicated that one of these complexes could also exist as a dimer.