MHC-BPS: MHC-binder prediction server for identifying peptides of flexible lengths from sequence-derived physicochemical properties

Juan Cui, Lian Yi Han, Hong Huang Lin, Zhi Qun Tang, Li Jiang, Zhi Wei Cao, Yu Zong Chen

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

Major histocompatibility complex (MHC)-binding peptides are essential for antigen recognition by T-cell receptors and are being explored for vaccine design. Computational methods have been developed for predicting MHC-binding peptides of fixed lengths, based on the training of relatively few non-binders. It is desirable to introduce methods applicable for peptides of flexible lengths and trained by using more diverse sets of non-binders. MHC-BPS is a web-based MHC-binder prediction server that uses support vector machines for predicting peptide binders of flexible lengths for 18 MHC class I and 12 class II alleles from sequence-derived physicochemical properties, which were trained by using 4,208-3,252 binders and 234,333-168,793 non-binders, and evaluated by an independent set of 545-476 binders and 110,564-84,430 non-binders. The binder prediction accuracies are 86-99% for 25 and 70-80% for five alleles, and the non-binder accuracies are 96-99% for 30 alleles. A screening of HIV-1 genome identifies 0.01-5% and 5-8% of the constituent peptides as binders for 24 and 6 alleles, respectively, including 75-100% of the known epitopes. This method correctly predicts 73.3% of the 15 newly published epitopes in the last 4 months of 2005. MHC-BPS is available at http://bidd.cz3.nus.edu.sg/mhc/.

Original languageEnglish (US)
Pages (from-to)607-613
Number of pages7
JournalImmunogenetics
Volume58
Issue number8
DOIs
StatePublished - Aug 2006
Externally publishedYes

Keywords

  • Epitopes
  • MHC-binding peptide
  • SVM

ASJC Scopus subject areas

  • Immunology
  • Genetics

Fingerprint

Dive into the research topics of 'MHC-BPS: MHC-binder prediction server for identifying peptides of flexible lengths from sequence-derived physicochemical properties'. Together they form a unique fingerprint.

Cite this