The E3/19K protein of adenovirus type 2 binds to the domains of histocompatibility antigens required for CTL recognition.
The E3/19K protein of human adenovirus type 2 binds to HLA class I antigens and blocks their terminal glycosylation and cell surface expression. The nature of this interaction is non-covalent and involves neither disulfide bridges between the two molecules nor their carbohydrates. The murine H-2 Kd antigen associates with the E3/19K protein in a similar fashion to human HLA antigens whereas the allelic product H-2 Kk does not. Hybrid genes between the Kd and Kk alleles were constructed and their products were expressed in embryonic kidney cells together with the E3/19K protein. This allowed us to identify the alpha 1 and alpha 2 domains as the essential structures of the histocompatibility antigens for binding the viral protein. Interestingly, these domains are also crucial for T cell recognition. The implications for the evolution of adenoviruses and their ability to cause persistent infections are discussed.
D017456:Adenovirus Early Proteins; D000260:Adenoviruses, Human / Q000235:genetics / Q000276:immunology*; D000818:Animals; D000957:Antigens, Viral, Tumor / Q000276:immunology*; D005075:Biological Evolution; D002460:Cell Line; D003602:Cytotoxicity, Immunologic; D006183:H-2 Antigens / Q000235:genetics / Q000276:immunology; D006680:HLA Antigens / Q000276:immunology*; D009856:Oncogene Proteins, Viral / Q000276:immunology*
D017456:Adenovirus Early Proteins; D000957:Antigens, Viral, Tumor; D006183:H-2 Antigens; D006680:HLA Antigens; D009856:Oncogene Proteins, Viral