Virus subversion of the MHC class I peptide-loading complex

Lonnie Lybarger, Xiaoli Wang, Michael R. Harris, Herbert W. Virgin IV, Ted H. Hansen

Research output: Contribution to journalArticlepeer-review

109 Scopus citations


Many viral proteins modulate class I expression, yet, in general, their mechanisms of specific class I recognition are poorly understood. The mK3 protein of γ2-Herpesvirus 68 targets the degradation of nascent class I molecules via the ubiquitin/proteasome pathway. Here, we identify cellular components of the MHC class I assembly machinery, TAP and tapasin, that are required for mK3 function. mK3 failed to regulate class I in TAP- or tapasin-deficient cells, and mK3 interacted with TAP/tapasin, even in the absence of class I. Expression of mK3 resulted in the ubiquitination of TAP/tapasin-associated class I, and mutants of class I incapable of TAP/tapasin interaction were unaffected by mK3. Thus, mK3 subverts TAP/tapasin to specifically target class I molecules for destruction.

Original languageEnglish (US)
Pages (from-to)121-130
Number of pages10
Issue number1
StatePublished - Jan 1 2003

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Infectious Diseases


Dive into the research topics of 'Virus subversion of the MHC class I peptide-loading complex'. Together they form a unique fingerprint.

Cite this