The Journal of Experimental Medicine
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Published online 19 June 2000.
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© The Rockefeller University Press, 0022-1007/2000/6/2083/ $5.00
The Journal of Experimental Medicine, Volume 191, Number 12, June 19, 2000 2083-2092

Original Article

An N-Acetylated Natural Ligand of Human Histocompatibility Leukocyte Antigen (Hla)-B39: Classical Major Histocompatibility Complex Class I Proteins Bind Peptides with a Blocked Nh2 Terminus in Vivo



Jesús Yagüea, Iñaki Alvareza, Didier Rognanb, Manuel Ramosa, Jesús Vázqueza, and José A. López de Castroa

a Centro de Biología Molecular Severo Ochoa, Universidad Autónoma de Madrid, Facultad de Ciencias, 28049 Madrid, Spain
b Department of Applied Biosciences, Eidgenössiche Technische Hochschule, CH-8057 Zürich, Switzerland
Centro de Biología Molecular <it>Severo Ochoa</it>, Universidad Autónoma de Madrid, Facultad de Ciencias, Cantoblanco, 28049 Madrid, Spain.34-91-397-80-8734-91-397-80-50

aldecastro{at}cbm.uam.es

Sequence-independent interactions involving the free peptidic NH2 terminus are thought to be an essential feature of peptide binding to classical major histocompatibility complex (MHC) class I proteins. Challenging this paradigm, a natural N{alpha}-acetylated ligand of human histocompatibility leukocyte antigen (HLA)-B39 was identified in this study. It matched the NH2-terminal sequence of two human helicases, was resistant to aminopeptidase M, and was produced with high yield from a synthetic 30 mer with the sequence of the putative parental protein by the 20S proteasome. This is the first reported natural ligand of classical MHC class I antigens that has a blocked NH2 terminus.

Key Words: human • antigen processing • biochemistry • molecular biology • tolerance

Abbreviations used in this paper: C1R, HMy2.C1R; MALDI-TOF, matrix-assisted laser desorption ionization time-of-flight; MS, mass spectrometry; NAc, N-acetyl.

© 2000 The Rockefeller University Press


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