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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 packaged into the virion resulting in reduced delivery of U L 26 to newly infected cells. Further, this C-terminal truncated U L 26 exhibited substantially reduced nuclear localization compared to wildtype U L 26. Translation of U L 26 mRNA is initiated from two separate in frame methionines that give rise to a long and a short isoform of U L 26. We find that the N-terminal 34 amino acids, which are unique to the long isoform of U L 26, are also important for the function of the U L 26 protein. A viral mutant that produces only the short isoform of U L 26 and lacks these N-terminal 34 amino acids exhibits delayed IE1 accumulation, and demonstrates intermediate defects in viral plaque size, virion stability and viral growth kinetics. Ablation of the short U L 26 isoform in the presence of the long U L 26 isoform did not impact any of the  in vitro  phenotypes tested. These experiments highlight important domains within the U L 26 protein that contribute to HCMV infection.

Distinct Domains within the Human Cytomegalovirus UL26 Protein Are Important for Wildtype Viral Replication and Virion Stability