Three-dimensional structure of a heteroclitic antigen-antibody cross-reaction complex. - Institut Pasteur Access content directly
Journal Articles Proceedings of the National Academy of Sciences of the United States of America Year : 1993

Three-dimensional structure of a heteroclitic antigen-antibody cross-reaction complex.

Pedro M. Alzari
Graham A. Bentley
  • Function : Author
T. Narayana Bhat
  • Function : Author
Jean-Luc Eiselé
  • Function : Author
A. Houdusse
Julien Lescar
Hélène Souchon
  • Function : Author
Roberto J. Poljak
  • Function : Author

Abstract

Although antibodies are highly specific, cross-reactions are frequently observed. To understand the molecular basis of this phenomenon, we studied the anti-hen egg lysozyme (HEL) monoclonal antibody (mAb) D11.15, which cross-reacts with several avian lysozymes, in some cases with a higher affinity (heteroclitic binding) than for HEL. We have determined the crystal structure of the Fv fragment of D11.15 complexed with pheasant egg lysozyme (PHL). In addition, we have determined the structure of PHL, Guinea fowl egg lysozyme, and Japanese quail egg lysozyme. Differences in the affinity of D11.15 for the lysozymes appear to result from sequence substitutions in these antigens at the interface with the antibody. More generally, cross-reactivity is seen to require a stereochemically permissive environment for the variant antigen residues at the antibody-antigen interface.

Dates and versions

pasteur-03136514 , version 1 (09-02-2021)

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Véronique Chitarra, Pedro M. Alzari, Graham A. Bentley, T. Narayana Bhat, Jean-Luc Eiselé, et al.. Three-dimensional structure of a heteroclitic antigen-antibody cross-reaction complex.. Proceedings of the National Academy of Sciences of the United States of America, 1993, 90 (16), pp.7711-7715. ⟨10.1073/pnas.90.16.7711⟩. ⟨pasteur-03136514⟩

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