, Volume 41, Issue 5, pp 257–262

Self peptides bound by HLA class I molecules are derived from highly conserved regions of a set of evolutionarily conserved proteins

  • Austin L. Hughes
  • Marianne K. Hughes

DOI: 10.1007/BF00172149

Cite this article as:
Hughes, A.L. & Hughes, M.K. Immunogenetics (1995) 41: 257. doi:10.1007/BF00172149


An evolutionary analysis of self peptides reported to be bound by HLA class I molecules showed that these peptides are largely derived from proteins that have been highly conserved in the history of mammals. These proteins also often have universal tissue expression and have a higher than average frequency of highly hydrophilic residues. The peptides themselves are generally still more highly conserved than the source proteins and have a higher frequency of highly hydrophobic residues, evidently often derived from conserved hydrophobic cores of the source proteins. These results suggest that the mechanism by which peptides are derived for MHC presentation may preferentially select peptides from conserved protein regions. In the case of parasite-derived peptides, such a mechanism would be adaptive in that it would reduce the likelihood of escape mutants.

Copyright information

© Springer-Verlag 1994

Authors and Affiliations

  • Austin L. Hughes
    • 1
  • Marianne K. Hughes
    • 2
  1. 1.Department of Biology, 208 Mueller LaboratoryThe Pennsylvania State UniversityUniversity ParkUSA
  2. 2.Institute of Molecular GeneticsThe Pennsylvania State UniversityUniversity ParkUSA