Identification and characterization of equine herpesvirus
نویسندگان
چکیده
19 Major histocompatibility complex class I (MHC-I) molecules play an important role in host 20 immunity to infection by presenting antigenic peptides to cytotoxic T lymphocytes (CTL), which 21 recognize and destroy virus-infected cells. Members of Herpesviridae have developed multiple 22 mechanisms to avoid CTL recognition by virtue of downregulation of MHC-I on the cell surface. 23 We report here on an immunomodulatory protein involved in this process, pUL56, which is encoded 24 by ORF1 of equine herpesvirus type 1 (EHV-1), an alphaherpesvirus. We show that EHV-1 pUL56 25 is a phosphorylated early protein, which is expressed as different forms and predominantly localizes 26 to Golgi membranes. In addition, the transmembrane (TM) domain of the type II membrane protein 27 was shown to be indispensable for correct subcellular localization and a proper function. pUL56 by 28 itself is not functional with respect to interference with MHC-I and likely needs (an)other 29 unidentified viral protein(s) to perform this action. Surprisingly, pUL49.5, an inhibitor of the 30 transporter associated with antigen processing (TAP) and encoded by EHV-1 and related viruses, 31 appeared not to be required for pUL56-induced early MHC-I downmodulation in infected cells. In 32 conclusion, our data identify a new immunomodulatory protein, pUL56, involved in MHC-I 33 downregulation, which is unable to perform its function outside of the context of viral infection. 34 35
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