The Journal of Experimental Medicine
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Published online 18 December 2000.
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© 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


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