Bovine hemesvirus 1 UL49.5 protein inhibits the transporter associated with antigen processing despite complex formation with glycoprotein M

A.D. Lipinska, D. Koppers-Lalic, M. Rychlowski, P. Admiraal, F.A.M. Rijsewijk, K. Bienkowska-Szewczyk, E. Wiertz

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    Abstract

    Bovine herpesvirus 1 (BHV-1) interferes with peptide translocation by the transporter associated with antigen processing (TAP). Recently, the UL49.5 gene product of BHV-1 was identified as the protein responsible for the observed inhibition of TAP. In BHV-1-infected cells and virions, the UL49.5 protein forms a complex with glycoprotein M (gM). Hence, it was investigated whether UL49.5 can combine the interactions with gM and the TAP complex. In cell lines constitutively expressing both UL49.5 and gM, UL49.5 appears to be required for functional processing of gM. Immunofluorescence-confocal laser scanning microscopy demonstrated that both proteins are interdependent for their redistribution from the endoplasmic reticulum to the trans-Golgi network. Remarkably, expression of cloned gM results in the abrogation of the UL49.5-mediated inhibition of TAP and prevents the degradation of the transporter. However, in BHV-1-infected cells, differences in UL49.5 and gM expression kinetics were seen to create a window of opportunity at the early stages of infection, during which time the UL49.5 protein can act on TAP without gM interference. Moreover, in later periods, non-gM-associated UL49.5 can be detected in addition to the UL49.5/gM complex. Thus, it has been deduced that different functions of UL49.5, editing of gM processing and inhibition of TAP, can be combined during BHV-1 infection.
    Original languageEnglish
    Pages (from-to)5822-5832
    JournalJournal of Virology
    Volume80
    Issue number12
    DOIs
    Publication statusPublished - 2006

    Keywords

    • peptide-loading complex
    • disulfide-linked complex
    • class-i molecules
    • to-cell spread
    • bovine herpesvirus-1
    • equine herpesvirus-1
    • pseudorabies virus
    • finger protein
    • homolog gene
    • gm homolog

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    Lipinska, A. D., Koppers-Lalic, D., Rychlowski, M., Admiraal, P., Rijsewijk, F. A. M., Bienkowska-Szewczyk, K., & Wiertz, E. (2006). Bovine hemesvirus 1 UL49.5 protein inhibits the transporter associated with antigen processing despite complex formation with glycoprotein M. Journal of Virology, 80(12), 5822-5832. https://doi.org/10.1128/JVI.02707-05