To study the genetic variation of human cytomegalovirus (HCMV) in Asian populations, the amino-terminal antigenic domains of glycoprotein B of HCMVs isolated from ethnic Chinese transplant patients were cloned and sequenced. The nucleotide and encoded amino acid sequences were compared with published sequences of AD169 and Towne laboratory strains. Within the region sequenced, 9 out of 15 clinical isolates (60%) possessed a peptide configuration similar to that of strain AD169 while 6 isolates (40%) displayed a peptide configuration similar to that of strain Towne. The nucleotide and amino acid identities of AD169-like clinical isolates exhibited variations of 95.4%-99.6% and 95.4%-100% respectively, whereas the identities of Towne-like clinical isolates were within the range of 97.3%-100% and 96.6%-100% at the nucleotide and amino acid levels. The previously defined neutralizing epitope was conserved among the clinical isolates sequenced while unique non-conservative amino acid substitutions were detected in the non-neutralizing epitope within the amino-terminal antigenic domain of glycoprotein B of all AD169-like isolates (Y- > S) and one of the Towne-like isolates (R- > Q).