Distinct domains within the human cytomegalovirus U(L)26 protein are important for wildtype viral replication and virion stability.

ABSTRACT: The human cytomegalovirus (HCMV) U(L)26 gene encodes a virion protein that is important for high titer viral replication. To identify specific domains within the U(L)26 protein that contribute to viral infection, we created a panel of site-directed U(L)26 mutant viruses and assessed their impact on phenotypes attributed to U(L)26. We find that the C-terminal 38 amino acids of the U(L)26 protein are absolutely necessary for U(L)26 function. A stop-insertion mutant that produced a truncated U(L)26 protein lacking this region behaved identically to U(L)26-null viruses. This included reduced accumulation of IE1 protein at early time points, smaller plaque size, reduced virion stability, and growth with similarly attenuated kinetics. This C-terminal truncation decreased the amount of U(L)26 pac

SUBMITTER: Mathers C 

PROVIDER: S-EPMC3914908 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature