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dc.contributor.authorVan Rhijn, Ildikoen_US
dc.contributor.authorYoung, David C.en_US
dc.contributor.authorDe Jong, Annemiekeen_US
dc.contributor.authorVazquez, Jennyen_US
dc.contributor.authorCheng, Tan-Yunen_US
dc.contributor.authorTalekar, Rahulen_US
dc.contributor.authorBarral, Duarte C.en_US
dc.contributor.authorLeón, Luisen_US
dc.contributor.authorBrenner, Michael B.en_US
dc.contributor.authorKatz, Joel T.en_US
dc.contributor.authorRiese, Richarden_US
dc.contributor.authorRuprecht, Ruth M.en_US
dc.contributor.authorO'Connor, Peter B.en_US
dc.contributor.authorCostello, Catherine E.en_US
dc.contributor.authorPorcelli, Steven A.en_US
dc.contributor.authorBriken, Volkeren_US
dc.contributor.authorMoody, D. Branchen_US
dc.date.accessioned2012-01-12T17:49:32Z
dc.date.available2012-01-12T17:49:32Z
dc.date.copyright2009
dc.date.issued2009-05-25
dc.identifier.citationVan Rhijn, Ildiko, David C. Young, Annemieke De Jong, Jenny Vazquez, Tan-Yun Cheng, Rahul Talekar, Duarte C. Barral, Luis León, Michael B. Brenner, Joel T. Katz, Richard Riese, Ruth M. Ruprecht, Peter B. O'Connor, Catherine E. Costello, Steven A. Porcelli, Volker Briken, D. Branch Moody. "CD1c bypasses lysosomes to present a lipopeptide antigen with 12 amino acids" Journal of Experimental Medicine 206(6): 1409-1422. (2009)
dc.identifier.issn1540-9538
dc.identifier.urihttps://hdl.handle.net/2144/3451
dc.description.abstractThe recent discovery of dideoxymycobactin (DDM) as a ligand for CD1a demonstrates how a nonribosomal lipopeptide antigen is presented to T cells. DDM contains an unusual acylation motif and a peptide sequence present only in mycobacteria, but its discovery raises the possibility that ribosomally produced viral or mammalian proteins that commonly undergo lipidation might also function as antigens. To test this, we measured T cell responses to synthetic acylpeptides that mimic lipoproteins produced by cells and viruses. CD1c presented an N-acyl glycine dodecamer peptide (lipo-12) to human T cells, and the response was specific for the acyl linkage as well as the peptide length and sequence. Thus, CD1c represents the second member of the CD1 family to present lipopeptides. lipo-12 was efficiently recognized when presented by intact cells, and unlike DDM, it was inactivated by proteases and augmented by protease inhibitors. Although lysosomes often promote antigen presentation by CD1, rerouting CD1c to lysosomes by mutating CD1 tail sequences caused reduction in lipo-12 presentation. Thus, although certain antigens require antigen processing in lysosomes, others are destroyed there, providing a hypothesis for the evolutionary conservation of large CD1 families containing isoforms that survey early endosomal pathways.en_US
dc.description.sponsorshipNational Institute of Allergy and Infectious Diseases (R01 AI049313, AI45889); National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01 AR048632); American Lung Association (RT-95-N); National Institutes of Health/National Center for Research Resources (P41 RR10888); Pew Foundation Scholars in the Biomedical Sciences; Burroughs Wellcome Fund Clinical Scientist Award in Translational Researchen_US
dc.language.isoen
dc.publisherThe Rockefeller University Pressen_US
dc.rightsCopyright 2009 Van Rhijn et al.en_US
dc.rights.urihttp://creativecommons.org/licenses/by/2.0/
dc.titleCD1c Bypasses Lysosomes to Present a Lipopeptide Antigen with 12 Amino Acidsen_US
dc.typeArticleen_US
dc.identifier.doi10.1084/jem.20082480
dc.identifier.pmid19468063
dc.identifier.pmcid2715062


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