The Journal of Experimental Medicine
Avanti Polar Lipids, Inc.
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

Published online 18 December 2000.
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 138K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JEM
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Zarling, A. L.
Right arrow Articles by Engelhard, V. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zarling, A. L.
Right arrow Articles by Engelhard, V. H.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?
© The Rockefeller University Press, 0022-1007/2000/12/1755/ $5.00
The Journal of Experimental Medicine, Volume 192, Number 12, December 18, 2000 1755-1762


Original Article

Phosphorylated Peptides Are Naturally Processed and Presented by Major Histocompatibility Complex Class I Molecules in Vivo

Angela L. Zarlinga, Scott B. Ficarrod, Forest M. Whited, Jeffrey Shabanowitzd, Donald F. Huntb,d, and Victor H. Engelharda,c

a Beirne B. Carter Center for Immunology Research, University of Virginia, Charlottesville, Virginia 22908
b Department of Pathology, University of Virginia, Charlottesville, Virginia 22908
c Department of Microbiology, University of Virginia, Charlottesville, Virginia 22908
d Department of Chemistry, University of Virginia, Charlottesville, Virginia 22901
Beirne Carter Center for Immunology Research, Medical Research Building 4, Box 801386, Charlottesville, VA 22908.804-924-1221804-924-2423

vhe{at}virginia.edu

Posttranslational modification of peptide antigens has been shown to alter the ability of T cells to recognize major histocompatibility complex (MHC) class I–restricted peptides. However, the existence and origin of naturally processed phosphorylated peptides presented by MHC class I molecules have not been explored. By using mass spectrometry, significant numbers of naturally processed phosphorylated peptides were detected in association with several human MHC class I molecules. In addition, CD8+ T cells could be generated that specifically recognized a phosphorylated epitope. Thus, phosphorylated peptides are part of the repertoire of antigens available for recognition by T cells in vivo.

Key Words: MHC class I • posttranslational protein processing • phosphopeptides • mass spectrometry • cytotoxic T lymphocytes


A.L. Zarling and S.B. Ficarro contributed equally to this work.

Abbreviations used in this paper: B-LCL, B lymphoblastoid cell line; c.eq., cell equivalents; DC, dendritic cell; ESI, electrospray ionization; IMAC, immobilized metal ion affinity chromatography; ID, inner diameter; MARCKS, myristoylated Ala-rich protein kinase C substrate; MS, mass spectrometry; OD, outer diameter; TAP, transporter associated with antigen processing.

© 2000 The Rockefeller University Press


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?




  Home | Help | Feedback | Subscriptions | Archive | Search
TABLE OF CONTENTS