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- Title
Structural insights into parallel strategies for germline antibody recognition of lipopolysaccharide from Chlamydia.
- Authors
Evans, Dylan W; Müller-Loennies, Sven; Brooks, Cory L; Brade, Lore; Kosma, Paul; Brade, Helmut; Evans, Stephen V
- Abstract
The structure of the antigen-binding fragment from the monoclonal antibody S64-4 in complex with a pentasaccharide bisphosphate fragment from chlamydial lipopolysaccharide has been determined by x-ray diffraction to 2.6 Å resolution. Like the well-characterized antibody S25-2, S64-4 displays a pocket formed by the residues of germline sequence corresponding to the heavy and light chain V gene segments that binds the terminal Kdo residue of the antigen; however, although S64-4 shares the same heavy chain V gene segment as S25-2, it has a different light chain V gene segment. The new light chain V gene segment codes for a combining site that displays greater affinity, different specificity, and allows a novel antigen conformation that brings a greater number of antigen residues into the combining site than possible in S25-2. Further, while antibodies in the S25-2 family use complementarity determining region (CDR) H3 to discriminate among antigens, S64-4 achieves its specificity via the new light chain V gene segment and resulting change in antigen conformation. These structures reveal an intriguing parallel strategy where two different combinations of germline-coded V gene segments can act as starting points for the generation of germline antibodies against chlamydial antigens and show how anti-carbohydrate antibodies can exploit the conformational flexibility of this class of antigens to achieve high affinity and specificity independently of CDR H3.
- Subjects
GERM cells; ENDOTOXINS; CHLAMYDIA; MOLECULAR structure; MONOCLONAL antibodies; PHOSPHATES; X-ray diffraction; ANTIGEN-antibody reactions; MOLECULAR recognition
- Publication
Glycobiology, 2011, Vol 21, Issue 8, p1049
- ISSN
0959-6658
- Publication type
Article
- DOI
10.1093/glycob/cwr041