This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Gerner, W.
Right arrow Articles by Saalmüller, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gerner, W.
Right arrow Articles by Saalmüller, A.

 Previous Article  |  Next Article 

Journal of Virology, May 2009, p. 4039-4050, Vol. 83, No. 9
0022-538X/09/$08.00+0     doi:10.1128/JVI.01534-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Identification of Major Histocompatibility Complex Restriction and Anchor Residues of Foot-and-Mouth Disease Virus-Derived Bovine T-Cell Epitopes{triangledown}

Wilhelm Gerner,1,2* Sabine E. Hammer,1 Karl-Heinz Wiesmüller,3 and Armin Saalmüller1,2

Institute of Immunology, Department of Pathobiology, University of Veterinary Medicine Vienna, Vienna, Austria,1 Friedrich-Loeffler-Institute, Federal Research Institute for Animal Health, Institute of Immunology, Tübingen, Germany,2 EMC Microcollections GmbH, Tübingen, Germany3

Received 21 July 2008/ Accepted 27 January 2009

Despite intensive research on the identification of T-cell epitopes in cattle after foot-and-mouth disease virus (FMDV) infection during the last 20 years, knowledge of major histocompatibility complex (MHC) restriction and anchor residues of such epitopes is still sparse. Therefore, as a first step, we tested lymphocytes from two experimentally FMDV serotype A24-vaccinated and -challenged cattle for recognition of FMDV-derived pentadecapeptides in proliferation assays. Two epitopes were identified: amino acid residues 66 to 80 within the structural protein 1D and amino acid residues 22 to 36 within the structural protein 1A. The latter epitope was recognized by lymphocytes from both cattle. Peptide-specific proliferation was caused by a response of CD4+ T helper cells as identified by carboxyfluorescein diacetate succinimidyl ester proliferation assays. Having identified one epitope that was recognized by two cattle, we hypothesized that these animals should have common MHC class II alleles. Cloning and sequencing of DRB3, DQA, and DQB alleles revealed that both animals possessed DQA allele 22021 and DQB allele 1301 but had no common DRB3 allele. A parallel analysis of amino acid residues involved in MHC presentation by peptides with alanine substitutions showed that the amino acid residues in positions 5 and 9 within the pentadecapeptide representing the 1A epitope were important for MHC binding in both cattle. These data indicate that the epitope located on FMDV protein 1A can be presented by MHC class II DQ molecules encoded by DQA allele 22021 and DQB allele 1301 and present the first evidence of the binding motif of this particular DQ molecule.

* Corresponding author. Mailing address: Institute of Immunology, Department of Pathobiology, University of Veterinary Medicine Vienna, Veterinärplatz 1, 1210 Vienna, Austria. Phone: 43-1-25077-2753. Fax: 43-1-25077-2791. E-mail: Wilhelm.Gerner{at}vu-wien.ac.at

{triangledown} Published ahead of print on 11 February 2009.

Journal of Virology, May 2009, p. 4039-4050, Vol. 83, No. 9
0022-538X/09/$08.00+0     doi:10.1128/JVI.01534-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»