CLONING AND SEQUENCE-ANALYSIS OF MURINE CYTOMEGALOVIRUS PROTEASE AND CAPSID ASSEMBLY PROTEIN GENES

The murine cytomegalovirus U(L)8O open reading frame was cloned and th e predicted amino acid sequence compared with those from other herpesv iruses. The open reading frame encodes a fused protease-capsid assembl y protein precursor and maintains conserved features including the act ive site serine, conserved regions CD1 through CD5, the release and ma turation sites, and a potential internal cleavage site within the prot ease. However, the murine cytomegalovirus protease differs in comparis on with the other proteases because it contains a unique 15-16 amino a cid insertion between CD3 and CD1. The assembly protein sequences are relatively divergent, but they can be arranged into groups defined by herpesvirus subfamily,with each group possessing a conserved motif at its carboxyl terminus. (C) 1994 Academic Press, Inc.