Human Cytomegalovirus Inhibits Tapasin-Dependent Peptide Loading and Optimization of the MHC Class I Peptide Cargo for Immune Evasion

Boyoun Park, Youngkyun Kim, Jinwook Shin, Sunray Lee, Kwangmin Cho, Klaus Früh, Sungwook Lee, Kwangseog Ahn

Research output: Contribution to journalArticlepeer-review

114 Scopus citations

Abstract

The immune evasion protein US3 of human cytomegalovirus binds to and arrests MHC class I molecules in the endoplasmic reticulum (ER). However, substantial amounts of class I molecules still escape US3-mediated ER retention, suggesting that not all class I alleles are affected equally by US3. Here, we identify tapasin inhibition as the mechanism of MHC retention by US3. US3 directly binds tapasin and inhibits tapasin-dependent peptide loading, thereby preventing the optimization of the peptide repertoire presented by class I molecules. Due to the allelic specificity of tapasin toward class I molecules, US3 affects only class I alleles that are dependent on tapasin for peptide loading and surface expression. Accordingly, tapasin-independent class I alleles selectively escape to the cell surface.

Original languageEnglish (US)
Pages (from-to)71-85
Number of pages15
JournalImmunity
Volume20
Issue number1
DOIs
StatePublished - Jan 2004

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Infectious Diseases

Fingerprint

Dive into the research topics of 'Human Cytomegalovirus Inhibits Tapasin-Dependent Peptide Loading and Optimization of the MHC Class I Peptide Cargo for Immune Evasion'. Together they form a unique fingerprint.

Cite this