Comparison of human cytomegalovirus (HCMV) protease sequences among laboratory strains and seven clinical isolates

Abstract

The nucleotide sequence of the human cytomegalovirus (HCMV) protease gene from two laboratory strains and seven clinical isolates, both ganciclovir-sensitive and -resistant, was examined to determine the genetic variability of the HCMV protease catalytic domain and to identify changes that may alter the efficacy of designed protease inhibitors. The Towne strain varied from AD169 at 12 nucleotides and led to one amino acid change at position 12 (Ala to Thr). The clinical isolates had amino acid substitutions relative to the laboratory strains, with a Ser to Pro change at position 8, a His to Tyr change at position 44 and a Gly to Ser change at position 47. None of these changes occurred in any of the conserved domains of the protease, nor do they appear necessary to confer ganciclovir resistance in the isolates. These findings suggest that no changes exist in the protease of the clinical isolates examined that may diminish the effectiveness of a drug targeting the HCMV protease.