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A TNF-like trimeric lectin domain from Burkholderia cenocepacia with specificity for fucosylated human histo-blood group antigens
O. Šulák, G. Cioci, M. Delia, M. Lahmann, A. Varrot, A. Imberty, M. Wimmerová
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
NLK
Cell Press Free Archives
from 1995-01-01 to 1 year ago
Free Medical Journals
from 1995 to 1 year ago
Free Medical Journals
from 1995 to 1 year ago
- MeSH
- Blood Group Antigens chemistry immunology metabolism MeSH
- Bacterial Proteins chemistry metabolism MeSH
- Burkholderia chemistry metabolism MeSH
- Epitopes chemistry immunology metabolism MeSH
- Fucose chemistry metabolism MeSH
- Protein Structure, Quaternary MeSH
- Lectins chemistry metabolism MeSH
- Humans MeSH
- Models, Molecular MeSH
- Molecular Sequence Data MeSH
- Amino Acid Sequence MeSH
- Sequence Alignment MeSH
- Binding Sites MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
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 BclA, the spore protein from Bacillus anthracis which may play an important role in bioadhesion of anthrax spores in human lungs.
References provided by Crossref.org
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