TAP mediates import of Mycobacterium tuberculosis-derived peptides into phagosomes and facilitates loading onto HLA-I

Melanie Harriff, Sven Burgdorf, Christian Kurts, Emmanuel J H J Wiertz, Deborah Lewinsohn, David Lewinsohn

Research output: Contribution to journalArticle

4 Scopus citations


Processing and presentation of antigen on MHC-I class I molecules serves to present peptides derived from cytosolic proteins to CD8+ T cells. Infection with bacteria that remain in phagosomal compartments, such as Mycobacterium tuberculosis (Mtb), provides a challenge to this immune recognition as bacterial proteins are segregated from the cytosol. Previously we identified the Mtb phagosome itself as an organelle capable of loading MHC Class I molecules with Mtb antigens. Here, we find that the TAP transporter, responsible for importing peptides into the ER for loading in Class I molecules, is both present and functional in Mtb phagosomes. Furthermore, we describe a novel peptide reagent, representing the N-terminal domain of the bovine herpes virus UL49.5 protein, which is capable of specifically inhibiting the lumenal face of TAP. Together, these results provide insight into the mechanism by which peptides from intra-phagosomal pathogens are loaded onto Class I molecules.

Original languageEnglish (US)
Article numbere79571
JournalPLoS One
Issue number11
Publication statusPublished - Nov 11 2013


ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

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