• We are sorry, but NCBI web applications do not support your browser and may not function properly. More information
Logo of pnasPNASInfo for AuthorsSubscriptionsAboutThis Article
Proc Natl Acad Sci U S A. May 1989; 86(9): 3296–3300.
PMCID: PMC287118

Prediction of major histocompatibility complex binding regions of protein antigens by sequence pattern analysis.

Abstract

We have previously experimentally analyzed the structural requirements for interaction between peptide antigens and mouse major histocompatibility complex (MHC) molecules of the d haplotype. We describe here two procedures devised to predict specifically the capacity of peptide molecules to interact with these MHC class II molecules (IAd and IEd). The accuracy of these procedures has been tested on a large panel of synthetic peptides of eukaryotic, prokaryotic, and viral origin, and also on a set of overlapping peptides encompassing the entire staphylococcal nuclease molecule. For both sets of peptides, IAd and IEd binding was successfully predicted in approximately 75% of the cases. This suggests that definition of such sequence "motifs" could be of general use in predicting potentially immunogenic peptide regions within proteins.

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (918K), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Sette A, Buus S, Colon S, Smith JA, Miles C, Grey HM. Structural characteristics of an antigen required for its interaction with Ia and recognition by T cells. Nature. 328(6129):395–399. [PubMed]
  • Sette A, Buus S, Colon S, Miles C, Grey HM. I-Ad-binding peptides derived from unrelated protein antigens share a common structural motif. J Immunol. 1988 Jul 1;141(1):45–48. [PubMed]
  • Adorini L, Sette A, Buus S, Grey HM, Darsley M, Lehmann PV, Doria G, Nagy ZA, Appella E. Interaction of an immunodominant epitope with Ia molecules in T-cell activation. Proc Natl Acad Sci U S A. 1988 Jul;85(14):5181–5185. [PMC free article] [PubMed]
  • Sette A, Buus S, Colon S, Miles C, Grey HM. Structural analysis of peptides capable of binding to more than one Ia antigen. J Immunol. 1989 Jan 1;142(1):35–40. [PubMed]
  • Guillet JG, Lai MZ, Briner TJ, Buus S, Sette A, Grey HM, Smith JA, Gefter ML. Immunological self, nonself discrimination. Science. 1987 Feb 20;235(4791):865–870. [PubMed]
  • Buus S, Sette A, Colon SM, Jenis DM, Grey HM. Isolation and characterization of antigen-Ia complexes involved in T cell recognition. Cell. 1986 Dec 26;47(6):1071–1077. [PubMed]
  • Rothbard JB, Taylor WR. A sequence pattern common to T cell epitopes. EMBO J. 1988 Jan;7(1):93–100. [PMC free article] [PubMed]
  • DeLisi C, Berzofsky JA. T-cell antigenic sites tend to be amphipathic structures. Proc Natl Acad Sci U S A. 1985 Oct;82(20):7048–7052. [PMC free article] [PubMed]
  • Margalit H, Spouge JL, Cornette JL, Cease KB, Delisi C, Berzofsky JA. Prediction of immunodominant helper T cell antigenic sites from the primary sequence. J Immunol. 1987 Apr 1;138(7):2213–2229. [PubMed]
  • Gammon G, Shastri N, Cogswell J, Wilbur S, Sadegh-Nasseri S, Krzych U, Miller A, Sercarz E. The choice of T-cell epitopes utilized on a protein antigen depends on multiple factors distant from, as well as at the determinant site. Immunol Rev. 1987 Aug;98:53–73. [PubMed]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

Formats:

Cited by other articles in PMC

See all...

Links

  • MedGen
    MedGen
    Related information in MedGen
  • PubMed
    PubMed
    PubMed citations for these articles
  • Substance
    Substance
    PubChem Substance links

Recent Activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...