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Blood, 27 August 2009, Vol. 114, No. 9, pp. 1954-1957. Prepublished online as a Blood First Edition Paper on June 3, 2009; DOI 10.1182/blood-2009-04-211839. This Article Full Text Full Text (PDF) All Versions of this Article: blood-2009-04-211839v1 114/9/1954    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Google Scholar Articles by Anani Sarab, G. Articles by Urbaniak, S. J. PubMed PubMed Citation Articles by Anani Sarab, G. Articles by Urbaniak, S. J. Related Collections Immunobiology Transfusion Medicine Platelets and Thrombopoiesis Brief Reports Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  TRANSFUSION MEDICINE Brief Report Naturally processed peptides spanning the HPA-1a polymorphism are efficiently generated and displayed from platelet glycoprotein by HLA-DRB3*0101–positive antigen-presenting cells Gholamreza Anani Sarab1,2, Michael Moss1,2,*, Robert N. Barker1,*, and Stanislaw J. Urbaniak1,2,* 1 Division of Applied Medicine, School of Medicine and Dentistry, University of Aberdeen, Aberdeen; and 2 Academic Transfusion Medicine Unit, Regional Transfusion Centre, Aberdeen, United Kingdom In neonatal alloimmune thrombocytopenia, almost all human platelet antigen (HPA)–1b1b mothers who produce anti–HPA-1a antibody through carrying an HPA-1a fetus are human histocompatibility leukocyte antigen (HLA)–DRB3*0101 positive. It is predicted that the HPA-1a Leu33 polymorphism forms part of an HLA-DRB3*0101–restricted T-helper epitope, and acts as an anchor residue for binding this class II molecule. However, it is not known whether any corresponding peptides are naturally processed and presented from platelet glycoprotein. In this study, peptides displayed by a homozygous HLA-DRB3*0101 antigen-presenting cell line were identified after pulsing with recombinant HPA-1a (Leu33 plexin-semaphorin-integrin domain). The peptides were eluted from HLA-DR molecules, fractionated by high performance liquid chromatography, and analyzed by tandem mass spectrometry. A "nested set" of naturally presented HPA-1a–derived peptides, each containing the Trp25-Leu33 core epitope, was identified, with the most abundant member being the 16-mer Met22-Arg37. These peptides may provide the basis for novel treatments to tolerize the corresponding T-helper response in women at risk of neonatal alloimmune thrombocytopenia. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: Processed platelet HPA1a peptides au naturel John W. Semple Blood 2009 114: 1724-1725. [Abstract] [Full Text] [PDF] This article has been cited by other articles: J. W. Semple Processed platelet HPA1a peptides au naturel Blood, August 27, 2009; 114(9): 1724 - 1725. [Abstract] [Full Text] [PDF]

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