期刊
STRUCTURE
卷 18, 期 1, 页码 59-72出版社
CELL PRESS
DOI: 10.1016/j.str.2009.10.021
关键词
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资金
- Ministry of Education [MSM0021622413, LC06030]
- Czech Republic [303/09/1168]
- CNRS
- French Ministry of Research
- European Community's Seventh Framework Programme [205872]
- French Ministry of Foreign and European Affairs [GDGD301/09/H004]
- Consortium for Functional Glycomics [GM62116]
- BARRANDE
- French cystic fibrosis association Vaincre la Mucoviscidose.
The opportunistic pathogen Burkholderia cenocepacia expresses several soluble lectins, among them BC2L-C. This lectin exhibits two domains: a C-terminal domain with high sequence similarity to the recently described calcium-dependent mannose-binding lectin BC2L-A, and an N-terminal domain of 156 amino acids without similarity to any known protein. The recombinant N-terminal BC2L-C domain is a new lectin with specificity for fucosylated human histo-blood group epitopes H-type 1, Lewis b, and Lewis Y, as determined by glycan array and isothermal titration calorimetry. Methylselenofucoside was used as ligand to solve the crystal structure of the N-terminal BC2L-C domain. Additional molecular modeling studies rationalized the preference for Lewis epitopes. The structure reveals a trimeric jellyroll arrangement with striking similarity to TNF-like proteins, and to BcIA, the spore protein from Bacillus anthracis which may play an important role in bioadhesion of anthrax spores in human lungs.
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