TAP mediates import of Mycobacterium tuberculosis-derived peptides into phagosomes and facilitates loading onto HLA-I.
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...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2013-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3823705?pdf=render |
| _version_ | 1828337505605255168 |
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| author | Melanie J Harriff Sven Burgdorf Christian Kurts Emmanuel J H J Wiertz Deborah A Lewinsohn David M Lewinsohn |
| author_facet | Melanie J Harriff Sven Burgdorf Christian Kurts Emmanuel J H J Wiertz Deborah A Lewinsohn David M Lewinsohn |
| author_sort | Melanie J Harriff |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-13T22:16:12Z |
| format | Article |
| id | doaj.art-1e4c350d380f45cd94d59df0f23b1a8f |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-04-13T22:16:12Z |
| publishDate | 2013-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-1e4c350d380f45cd94d59df0f23b1a8f2022-12-22T02:27:30ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-01811e7957110.1371/journal.pone.0079571TAP mediates import of Mycobacterium tuberculosis-derived peptides into phagosomes and facilitates loading onto HLA-I.Melanie J HarriffSven BurgdorfChristian KurtsEmmanuel J H J WiertzDeborah A LewinsohnDavid M LewinsohnProcessing 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.http://europepmc.org/articles/PMC3823705?pdf=render |
| spellingShingle | Melanie J Harriff Sven Burgdorf Christian Kurts Emmanuel J H J Wiertz Deborah A Lewinsohn David M Lewinsohn TAP mediates import of Mycobacterium tuberculosis-derived peptides into phagosomes and facilitates loading onto HLA-I. PLoS ONE |
| title | TAP mediates import of Mycobacterium tuberculosis-derived peptides into phagosomes and facilitates loading onto HLA-I. |
| title_full | TAP mediates import of Mycobacterium tuberculosis-derived peptides into phagosomes and facilitates loading onto HLA-I. |
| title_fullStr | TAP mediates import of Mycobacterium tuberculosis-derived peptides into phagosomes and facilitates loading onto HLA-I. |
| title_full_unstemmed | TAP mediates import of Mycobacterium tuberculosis-derived peptides into phagosomes and facilitates loading onto HLA-I. |
| title_short | TAP mediates import of Mycobacterium tuberculosis-derived peptides into phagosomes and facilitates loading onto HLA-I. |
| title_sort | tap mediates import of mycobacterium tuberculosis derived peptides into phagosomes and facilitates loading onto hla i |
| url | http://europepmc.org/articles/PMC3823705?pdf=render |
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