Key result
In two FMDV-vaccinated cattle, two T-cell epitopes were identified within structural proteins 1D and 1A, with the 1A epitope presented by MHC class II DQ molecules using anchor residues at positions 5 and 9.
The study identifies specific FMDV T-cell epitopes and their MHC class II restriction in cattle, providing the first evidence of the binding motif for a specific bovine DQ molecule.
May inform bovine FMDV epitope vaccine design; leaves open translation without larger validation studies.
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.
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Gerner et al. (2009) studied Foot-and-mouth disease virus (FMDV) infection (n=2). FMDV-derived pentadecapeptides vs. Control peptide or medium was evaluated on T-cell epitope recognition (lymphocyte proliferation and IFN-γ production). In two FMDV-vaccinated cattle, two T-cell epitopes were identified within structural proteins 1D and 1A, with the 1A epitope presented by MHC class II DQ molecules using anchor residues at positions 5 and 9.
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