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Taxonomic group: bacteria / Chlamydiae (Phylum: Chlamydiae)
Associated disease: infection due to Chlamydia psittaci [ICD11: XN4S7

]

NCBI PubMed ID: 21543444
Publication DOI: 10.1093/glycob/cwr041
Journal NLM ID: 9104124
Publisher: IRL Press at Oxford University Press
Correspondence: hebra

fz-borstel.de; svenvans

uvic.ca
Institutions: Department of Biochemistry and Microbiology, University of Victoria, PO Box 3055 STN CSC, Victoria, BC, Canada V8P 3P6, Research Center Borstel, Leibniz-Center for Medicine and Biosciences, Parkallee 22, Borstel D-23845, Germany, Department of Chemistry, University of Natural Resources and Life Sciences, Vienna A-1190, Austria

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 A 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.

Chlamydia, crystal structure, carbohydrate antigen, antibody-antigen recognition, chlamydial LPS, germline antibody

Structure type: oligomer
Location inside paper: p.1050, fig.1
Trivial name: cross-reactive epitope
Compound class: core oligosaccharide, LPS
Contained glycoepitopes: IEDB_130650,IEDB_130657,IEDB_130658,IEDB_130659,IEDB_135394,IEDB_135515,IEDB_140092,IEDB_141807,IEDB_150755,IEDB_150756,IEDB_150760,IEDB_150901,IEDB_150908,IEDB_151531,IEDB_151769,IEDB_176772,IEDB_534865

Methods: X-ray, ELISA, serological methods
Biological activity: serological data
Biosynthesis and genetic data: genetic data
3D data: 3D data

NCBI Taxonomy refs (TaxIDs): 83554
Show glycosyltransferases

There is only one chemically distinct structure:

CCCCCCCCCCCCCCCCCC(=O)OC(CCCCCCCCCCCCCCCCC)CC(=O)N[C@H]1[C@H](OC[C@H]2O[C@H](OP(=O)(O)O)[C@H](NC(=O)CC(O)CCCCCCCCCCCCCCCCC)[C@@H](OC(=O)CCCCCCCCCCCCC)[C@@H]2O)O[C@H](CO[C@]2(C(=O)O)C[C@@H](O[C@]3(C(=O)O)C[C@@H](O[C@]4(C(=O)O)C[C@@H](O)[C@@H](O)[C@@H]([C@H](O)CO)O4)[C@@H](O)[C@@H]([C@H](O)CO[C@]4(C(=O)O)C[C@@H](O)[C@@H](O)[C@@H]([C@H](O)CO)O4)O3)[C@@H](O)[C@@H]([C@H](O)CO)O2)[C@@H](OP(=O)(O)O)[C@@H]1OC(=O)CCCCCCCCCCCCC

SVG MW SMILES 3D mol Ionize