The Influence of MHC Polymorphism on the Selection of T-cell Determinants of FMDV in Cattle

Overview

Journal Immunology

Specialty Allergy & Immunology

Date 1995 Jan 1

PMID 7534267

Citations 9

Authors

M J van Lierop

P R Nilsson

J P WAGENAAR

J M van Noort

J D Campbell

E J Glass

I Joosten

E J Hensen

Affiliations

Soon will be listed here.

Abstract

There is a quest for the development of a new generation of vaccines consisting of well-defined subunit antigens. For a number of practical reasons it is attractive to develop vaccines on the basis of synthetic peptides. However, their efficacy may be limited by genetic restrictions imposed on T-cell recognition via major histocompatibility complex (MHC) polymorphism, as shown by many studies using inbred animal species. To study the effect of MHC polymorphism in an outbred species, we selected four cattle homozygous for different A-DR-DQ haplotypes, and another four cattle which shared one haplotype in combination with a haplotype of one of the MHC homozygous animals. We analysed responses to synthetic peptides comprising defined T-cell epitopes of foot-and-mouth disease virus (FMDV) in this selected group of FMDV-vaccinated cattle. This analysis shows that even in outbred animals. MHC polymorphism influences the responses to synthetic peptides. Interestingly, one of the peptides, VP4[20-34], was recognized in association with at least four different MHC haplotypes. Fine specificity analysis of this peptide revealed subtle shifts in the core epitope recognized. All peptides that induced lymphocyte proliferation in vitro were found to induce a T-helper type-1 (Th1) type of response, irrespective of the MHC haplotype involved. Together, these data support the notion that individuals carrying distinct MHC types can be vaccinated successfully by vaccines that include only a limited number of peptides. In the design of a peptide vaccine against FMDV we suggest inclusion of the highly conserved VP4 sequence 20-34.

Citing Articles

The detection of long-lasting memory foot-and-mouth disease (FMD) virus serotype O-specific CD4 T cells from FMD-vaccinated cattle by bovine major histocompatibility complex class II tetramer.

Mitoma S, Carr B, Harvey Y, Moffat K, Sekiguchi S, Charleston B Immunology. 2021; 164(2):266-278.

PMID: 34003490 PMC: 8442236. DOI: 10.1111/imm.13367.

Molecular Mechanisms of Immune Escape for Foot-and-Mouth Disease Virus.

Yang B, Zhang X, Zhang D, Hou J, Xu G, Sheng C Pathogens. 2020; 9(9).

PMID: 32899635 PMC: 7558374. DOI: 10.3390/pathogens9090729.

Identification of major histocompatibility complex restriction and anchor residues of foot-and-mouth disease virus-derived bovine T-cell epitopes.

Gerner W, Hammer S, Wiesmuller K, Saalmuller A J Virol. 2009; 83(9):4039-50.

PMID: 19211750 PMC: 2668444. DOI: 10.1128/JVI.01534-08.

Assessment of cross-reactivity between Mycobacterium bovis and M. kansasii ESAT-6 and CFP-10 at the T-cell epitope level.

Vordermeier H, Brown J, Cockle P, Franken W, Drijfhout J, Arend S Clin Vaccine Immunol. 2007; 14(9):1203-9.

PMID: 17671227 PMC: 2043317. DOI: 10.1128/CVI.00116-07.

Quantitation of Anaplasma marginale major surface protein (MSP)1a and MSP2 epitope-specific CD4+ T lymphocytes using bovine DRB3*1101 and DRB3*1201 tetramers.

Norimine J, Han S, Brown W Immunogenetics. 2006; 58(9):726-39.

PMID: 16924490 DOI: 10.1007/s00251-006-0140-3.

References

van Rood J, van Leeuwen A, Ploem J . Simultaneous detection of two cell populations by two-colour fluorescence and application to the recognition of B-cell determinants. Nature. 1976; 262(5571):795-7. DOI: 10.1038/262795a0. View

Davies C, Joosten I, Andersson L, Arriens M, Bernoco D, Bissumbhar B . Polymorphism of bovine MHC class II genes. Joint report of the Fifth International Bovine Lymphocyte Antigen (BoLA) Workshop, Interlaken, Switzerland, 1 August 1992. Eur J Immunogenet. 1994; 21(4):259-89. DOI: 10.1111/j.1744-313x.1994.tb00198.x. View

Shastri N, Oki A, Miller A, Sercarz E . Distinct recognition phenotypes exist for T cell clones specific for small peptide regions of proteins. Implications for the mechanisms underlying major histocompatibility complex-restricted antigen recognition and clonal deletion models of immune.... J Exp Med. 1985; 162(1):332-45. PMC: 2187680. DOI: 10.1084/jem.162.1.332. View

Schwartz R . T-lymphocyte recognition of antigen in association with gene products of the major histocompatibility complex. Annu Rev Immunol. 1985; 3:237-61. DOI: 10.1146/annurev.iy.03.040185.001321. View

Reeves R, Spies A, Nissen M, Buck C, Weinberg A, Barr P . Molecular cloning of a functional bovine interleukin 2 cDNA. Proc Natl Acad Sci U S A. 1986; 83(10):3228-32. PMC: 323486. DOI: 10.1073/pnas.83.10.3228. View

Andersson L, Bohme J, Rask L, Peterson P . Genomic hybridization of bovine class II major histocompatibility genes: 1. Extensive polymorphism of DQ alpha and DQ beta genes. Anim Genet. 1986; 17(2):95-112. DOI: 10.1111/j.1365-2052.1986.tb00731.x. View

Andersson L, Bohme J, Peterson P, Rask L . Genomic hybridization of bovine class II major histocompatibility genes: 2. Polymorphism of DR genes and linkage disequilibrium in the DQ-DR region. Anim Genet. 1986; 17(4):295-304. DOI: 10.1111/j.1365-2052.1986.tb00723.x. View

Andersson L, Rask L . Characterization of the MHC class II region in cattle. The number of DQ genes varies between haplotypes. Immunogenetics. 1988; 27(2):110-20. DOI: 10.1007/BF00351084. View

Andersson L, Lunden A, Sigurdardottir S, Davies C, Rask L . Linkage relationships in the bovine MHC region. High recombination frequency between class II subregions. Immunogenetics. 1988; 27(4):273-80. DOI: 10.1007/BF00376122. View

10.

Francis M, Fry C, Rowlands D, Brown F . Qualitative and quantitative differences in the immune response to foot-and-mouth disease virus antigens and synthetic peptides. J Gen Virol. 1988; 69 ( Pt 10):2483-91. DOI: 10.1099/0022-1317-69-10-2483. View

11.

Sinigaglia F, Guttinger M, Kilgus J, Doran D, Matile H, Etlinger H . A malaria T-cell epitope recognized in association with most mouse and human MHC class II molecules. Nature. 1988; 336(6201):778-80. DOI: 10.1038/336778a0. View

12.

Joosten I, Sanders M, van der Poel A, Williams J, Hepkema B, Hensen E . Biochemically defined polymorphism of bovine MHC class II antigens. Immunogenetics. 1989; 29(3):213-6. DOI: 10.1007/BF00373649. View

13.

Glass E, SPOONER R . Requirement for MHC class II positive accessory cells in an antigen specific bovine T cell response. Res Vet Sci. 1989; 46(2):196-201. View

14.

Mosmann T, Coffman R . TH1 and TH2 cells: different patterns of lymphokine secretion lead to different functional properties. Annu Rev Immunol. 1989; 7:145-73. DOI: 10.1146/annurev.iy.07.040189.001045. View

15.

Wiesmuller K, Jung G, Hess G . Novel low-molecular-weight synthetic vaccine against foot-and-mouth disease containing a potent B-cell and macrophage activator. Vaccine. 1989; 7(1):29-33. DOI: 10.1016/0264-410x(89)90007-8. View

16.

Glass E, Oliver R, SPOONER R . Variation in T cell responses to ovalbumin in cattle: evidence for Ir gene control. Anim Genet. 1990; 21(1):15-28. DOI: 10.1111/j.1365-2052.1990.tb03203.x. View

17.

Rothel J, Jones S, Corner L, Cox J, Wood P . A sandwich enzyme immunoassay for bovine interferon-gamma and its use for the detection of tuberculosis in cattle. Aust Vet J. 1990; 67(4):134-7. DOI: 10.1111/j.1751-0813.1990.tb07730.x. View

18.

Kilgus J, Jardetzky T, Gorga J, Trzeciak A, Gillessen D, Sinigaglia F . Analysis of the permissive association of a malaria T cell epitope with DR molecules. J Immunol. 1991; 146(1):307-15. View

19.

Collen T, DiMarchi R, Doel T . A T cell epitope in VP1 of foot-and-mouth disease virus is immunodominant for vaccinated cattle. J Immunol. 1991; 146(2):749-55. View

20.

Glass E, Oliver R, Collen T, Doel T, DiMarchi R, SPOONER R . MHC class II restricted recognition of FMDV peptides by bovine T cells. Immunology. 1991; 74(4):594-9. PMC: 1384766. View