KSHV-K5 inhibits phosphorylation of the major histocompatibility complex class I cytoplasmic tail

Emily Paulson, Chinh Tran, Kathleen Collins, Klaus Früh

Research output: Contribution to journalArticle

19 Scopus citations

Abstract

The carboxy-terminal region of major histocompatibility complex class I (MHC I) molecules is required for the rapid internalization mediated by Kaposi's sarcoma-associated herpesvirus (KSHV) proteins K3 and K5, The cytoplasmic tail of MHC I contains highly conserved serine phosphorylation sites that have been implicated in intracellular trafficking. Indeed, in vivo labeling experiments reveal a lack of MHC I phosphorylation in K5-transfected HeLa cells. Phosphorylation of the MHC I tail was restored upon mutation of the PHD/LAP domain of K5. However, deletion and mutation studies of the MHC I tail show that both K3 and K5 are able to downregulate MHC I lacking the conserved phosphorylation site. This result suggests that inhibition of phosphorylation reflects, but does not cause, MHC I internalization. Interestingly, K3 and K5 differ from each other, as well as from human immunodeficiency virus nef, with respect to the minimal MHC I tail sequences required for MHC downregulation. These data support the notion that K3 and K5 downregulate MHC I molecules by a distinct molecular mechanism that is different from other viral immune evasion molecules.

Original languageEnglish (US)
Pages (from-to)369-378
Number of pages10
JournalVirology
Volume288
Issue number2
DOIs
StatePublished - Sep 30 2001

Keywords

  • HHV8
  • Immune escape
  • Intracellular transport
  • KSHV
  • Kaposi's sarcoma
  • Major histocompatibility complex class I
  • Serine phosphorylation

ASJC Scopus subject areas

  • Virology

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