Promiscuous and allele-specific anchors in HLA-DR-binding peptides - PubMed (original) (raw)
Promiscuous and allele-specific anchors in HLA-DR-binding peptides
J Hammer et al. Cell. 1993.
Abstract
The major histocompatibility complex (MHC) class II molecules are highly polymorphic membrane glycoproteins that bind peptide fragments of proteins and display them for recognition by CD4+ T cells. To understand the effect of human MHC class II polymorphism on peptide-MHC interaction, we have isolated M13 phage from a large M13 peptide display library by selection with DRB1*0401 and DRB1*1101 molecules, as recently described for DRB1*0101. Sequence analysis of the peptide-encoding region of DR-bound phage led to the identification of position-specific anchor residues, defining motifs for peptide binding to DR molecules. The three DR motifs share two anchor residues at relative positions 1 and 4, while allele-specific anchor residues have been identified at position 6. These results provide a biophysical basis for both the promiscuity and the specificity of peptide recognition by DR molecules.
Similar articles
- Analysis of peptide-binding motifs for two disease associated HLA-DR13 alleles using an M13 phage display library.
Davenport MP, Quinn CL, Valsasnini P, Sinigaglia F, Hill AV, Bell JI. Davenport MP, et al. Immunology. 1996 Aug;88(4):482-6. doi: 10.1046/j.1365-2567.1996.d01-693.x. Immunology. 1996. PMID: 8881746 Free PMC article. - High-affinity binding of short peptides to major histocompatibility complex class II molecules by anchor combinations.
Hammer J, Belunis C, Bolin D, Papadopoulos J, Walsky R, Higelin J, Danho W, Sinigaglia F, Nagy ZA. Hammer J, et al. Proc Natl Acad Sci U S A. 1994 May 10;91(10):4456-60. doi: 10.1073/pnas.91.10.4456. Proc Natl Acad Sci U S A. 1994. PMID: 8183931 Free PMC article. - Ligand motifs of HLA-DRB5*0101 and DRB1*1501 molecules delineated from self-peptides.
Vogt AB, Kropshofer H, Kalbacher H, Kalbus M, Rammensee HG, Coligan JE, Martin R. Vogt AB, et al. J Immunol. 1994 Aug 15;153(4):1665-73. J Immunol. 1994. PMID: 7519208 - Defining rules for the peptide-MHC class II interaction.
Sinigaglia F, Hammer J. Sinigaglia F, et al. Curr Opin Immunol. 1994 Feb;6(1):52-6. doi: 10.1016/0952-7915(94)90033-7. Curr Opin Immunol. 1994. PMID: 7513526 Review. - Class I MHC-peptide interaction: structural and functional aspects.
Ruppert J, Kubo RT, Sidney J, Grey HM, Sette A. Ruppert J, et al. Behring Inst Mitt. 1994 Jul;(94):48-60. Behring Inst Mitt. 1994. PMID: 7998914 Review.
Cited by
- Plasmodium vivax promiscuous T-helper epitopes defined and evaluated as linear peptide chimera immunogens.
Caro-Aguilar I, Rodríguez A, Calvo-Calle JM, Guzmán F, De la Vega P, Patarroyo ME, Galinski MR, Moreno A. Caro-Aguilar I, et al. Infect Immun. 2002 Jul;70(7):3479-92. doi: 10.1128/IAI.70.7.3479-3492.2002. Infect Immun. 2002. PMID: 12065487 Free PMC article. - A hybrid approach for predicting promiscuous MHC class I restricted T cell epitopes.
Bhasin M, Raghava GP. Bhasin M, et al. J Biosci. 2007 Jan;32(1):31-42. doi: 10.1007/s12038-007-0004-5. J Biosci. 2007. PMID: 17426378 - Measurement of MHC/peptide interactions by gel filtration or monoclonal antibody capture.
Sidney J, Southwood S, Moore C, Oseroff C, Pinilla C, Grey HM, Sette A. Sidney J, et al. Curr Protoc Immunol. 2013 Feb;Chapter 18:Unit 18.3.. doi: 10.1002/0471142735.im1803s100. Curr Protoc Immunol. 2013. PMID: 23392640 Free PMC article. - Molecular mimicry and T cell-mediated autoimmune disease.
Barnaba V, Sinigaglia F. Barnaba V, et al. J Exp Med. 1997 May 5;185(9):1529-31. doi: 10.1084/jem.185.9.1529. J Exp Med. 1997. PMID: 9151889 Free PMC article. Review. No abstract available. - Analysis of anchor residues in a naturally processed HLA-DR53 ligand.
Kobayashi H, Kokubo T, Abe Y, Sato K, Kimura S, Miyokawa N, Katagiri M. Kobayashi H, et al. Immunogenetics. 1996;44(5):366-71. doi: 10.1007/BF02602781. Immunogenetics. 1996. PMID: 8781122
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Research Materials