FASEB J. Thermo Fisher Scientific
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Sela, M.
Right arrow Articles by Zisman, E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sela, M.
Right arrow Articles by Zisman, E.

The FASEB Journal, Vol 11, 449-456, Copyright © 1997 by The Federation of American Societies for Experimental Biology

REVIEWS

Different roles of D-amino acids in immune phenomena

M Sela and E Zisman
Department of Immunology, The Weizmann Institute of Science, Rehovot, Israel.

Peptides and polypeptides either fully or partially built of D-amino acids interest researchers because of their advantages over all L peptides and polypeptides. In exploiting these characteristics, one should realize that the resulting molecules are nonetheless not inert, but rather may induce a unique immune response, which is hardly cross- reactive with the L-enantiomer. Moreover, cross-reaction between the L- and the D-sequences is limited also at the T cell level, probably due to different sterical conformations of the MHC-antigen-T cell receptor complexes formed. Polypeptides built exclusively of D-amino acids lead to antibody formation only at a relatively low concentration, otherwise they provoke immunological paralysis. The specificity of the immune response toward peptides containing D-amino acid residues is exquisite, and often D-amino acids play a dominant role in defining the specificity. Polypeptides composed exclusively of D-amino acids are thymus-independent antigens. Nevertheless, it is possible to prepare against them highly specific T cell hybridomas. In future plans for synthetic vaccines against infectious or autoimmune diseases, the inclusion of D-amino acids may be an advantage in terms of both specificity and efficacy, the latter because of longer persistence in an undigested form because they resist enzymatic degradation.


This article has been cited by other articles:


Home page
 Proc. Natl. Acad. Sci. USAHome page
R. Tugyi, K. Uray, D. Ivan, E. Fellinger, A. Perkins, and F. Hudecz
Partial D-amino acid substitution: Improved enzymatic stability and preserved Ab recognition of a MUC2 epitope peptide
PNAS, January 11, 2005; 102(2): 413 - 418.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Sela
From Proteins and Protein Models to Their Use in Immunology and Immunotherapy
J. Biol. Chem., December 5, 2003; 278(49): 48507 - 48519.
[Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
N. Chamond, C. Gregoire, N. Coatnoan, C. Rougeot, L. H. Freitas-Junior, J. F. da Silveira, W. M. Degrave, and P. Minoprio
Biochemical Characterization of Proline Racemases from the Human Protozoan Parasite Trypanosoma cruzi and Definition of Putative Protein Signatures
J. Biol. Chem., April 25, 2003; 278(18): 15484 - 15494.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
J. R. Sydor, C. Herrmann, S. B. H. Kent, R. S. Goody, and M. Engelhard
Design, total chemical synthesis, and binding properties of a [Leu-91-N1-methyl-7-azaTrp]Ras-binding domain of c-Raf-1
PNAS, July 6, 1999; 96(14): 7865 - 7870.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1997 by The Federation of American Societies for Experimental Biology.