| Abstract
| - The complete envelope glycoprotein H (gH) coding sequences of 10 clinical strains of cytomegalovirus (CMV) were determined and compared with those of laboratory strains AD169 and Towne. Their translated peptide sequences segregated into two groups, exemplified by AD169 and Towne. Peptide variation was mostly group-specific and was clustered in the first 37 amino acids, including the signal sequence; in the rest of the molecule, there were scattered amino acid substitutions, usually in single residues. Compared with CMV envelope glycoprotein B, gH is more highly conserved among strains and may be expected to have limited immunologic diversity.
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