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© Institut Pasteur
Cells infected for 24 hrs with C. Trachomatis. The cell nuclei are labelled in blue, the bacteria appear yellow, within the inclusion lumen. A bacterial protein secreted out the inclusion into the host cytoplasm id labelled in red.
Publication : Proceedings of the National Academy of Sciences of the United States of America

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Proceedings of the National Academy of Sciences of the United States of America - 15 Aug 1993

Chitarra V, Alzari PM, Bentley GA, Bhat TN, Eiselé JL, Houdusse A, Lescar J, Souchon H, Poljak RJ

Link to Pubmed [PMID] – 8356074

Proc. Natl. Acad. Sci. U.S.A. 1993 Aug;90(16):7711-5

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.

http://www.ncbi.nlm.nih.gov/pubmed/8356074