MHC Molecules: Expression, Assembly and Function

  • Robert G. Urban
  • Roman M. Chicz

Table of contents

  1. Front Matter
    Pages i-xi
  2. Roman M. Chicz, Robert G. Urban
    Pages 1-8
  3. Sarki A. Abdulkadir, Vincenzo Casolaro, Lisa S. Schwiebert, Zhimin Song, Santa Jeremy Ono
    Pages 9-34
  4. Frank Momburg, Günter J. Hämmerling, Jacques J. Neefjes
    Pages 35-63
  5. Lois Isenman
    Pages 73-82
  6. Alexander Y. Rudensky
    Pages 83-96
  7. Tom Cotner, Donald Pious
    Pages 97-111
  8. Joan C. Gorga, Dimitri Monos
    Pages 135-162
  9. Stephen C. Jameson, Kristin A. Hogquist
    Pages 181-190
  10. Theodore J. Tsomides
    Pages 191-206
  11. Miles P. Davenport, Adrian V. S. Hill
    Pages 243-260
  12. Charlotte Hetzel, Gerard F. Hoyne, Nanna M. Kristensen, Timothy Bourne, Daphne Tsitoura, Jonathan R. Lamb
    Pages 261-279
  13. Mary Lynne Hedley
    Pages 281-294
  14. Back Matter
    Pages 295-298

About this book


3 nant expression systems have been used to make MHC molecules con­ taining a single peptide of interest. To date, fifteen single peptide class I structures (incorporating three different HLA and two different H-2 allotypes/isotypes) and four additional class II structures (two single peptide complexes and two superantigen complexes) have been reported. These advances have enabled us to study the atomic detail of antigen presentation and the general mechanisms behind peptide binding, and begin to construct models of T cell recognition. Another area of research which has exploded over the past five years has been the identification of MHC-associated peptides. There are several methods one can use to determine the sequence identity of MHC restricted peptides. Historically, the most successful technique, albeit crude and encumbered with serious limitations, has been the use of overlapping synthetic peptides and T cell clones. Unfortunately, this method absolutely requires: (i) knowledge of the target antigen; (ii) availability of T cell clones; and (iii) a relatively short overall length for the target source protein, such that a set of overlapping pep tides can be affordably synthesized. Briefly, the entire sequence of the tar­ get protein is chemically synthesized using overlapping peptides which are then screened for biological activity using standard T cell presen­ tation assays. Despite its limitations, this method was used to identify the first immunodominant epitopes reported in the literature and con­ tinues to be used successfully today.


T cell antigen antigen presentation autoimmune disease cognition cytotoxicity diseases evolution histocompatibility identity immunization immunoglobulin research vaccine

Authors and affiliations

  • Robert G. Urban
    • 1
  • Roman M. Chicz
    • 1
  1. 1.Harvard UniversityCambridgeUSA

Bibliographic information