The herpes simplex virus 1 UL26 gene encodes a protease that catalyzes its own cleavage and that of the UL26.5 product at a site approximately 20 amino acids from their carboxyl termini.
The study identifies that the HSV-1 UL26 gene encodes a protease responsible for cleaving itself and the UL26.5 product near their carboxyl termini.
The herpes simplex virus 1 open reading frames UL26 and UL26.5 are 3' coterminal. The larger, UL26 open reading frame encodes a protein approximately 80,000 in apparent molecular weight and contains the promoter and coding sequence of the UL26.5 gene, which specifies a capsid protein designated infected cell protein 35. The larger product contains in its entirety the amino acid sequence of the smaller protein. We report that the UL26 gene encodes a protease which catalyzes its own cleavage and that of the more abundant product of UL26.5. By inserting the coding sequence of an epitope to a cytomegalovirus monoclonal antibody and homologs of the immunoglobulin G binding domain of staphylococcal protein A into the 3' termini of the coding domains of the two open reading frames, we identified both products of the cleavage and determined that the cleavage site is approximately 20 amino acids from the carboxyl termini of both proteins.
Liu et al. (Tue,) conducted a other in Herpes simplex virus 1. The herpes simplex virus 1 UL26 gene encodes a protease that catalyzes its own cleavage and that of the UL26.5 product at a site approximately 20 amino acids from their carboxyl termini.