A TNF-like trimeric lectin domain from Burkholderia cenocepacia with specificity for fucosylated human histo-blood group antigens

Structure. 2010 Jan 13;18(1):59-72. doi: 10.1016/j.str.2009.10.021.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Blood Group Antigens / chemistry*
  • Blood Group Antigens / immunology
  • Blood Group Antigens / metabolism
  • Burkholderia / chemistry*
  • Burkholderia / metabolism
  • Epitopes / chemistry
  • Epitopes / immunology
  • Epitopes / metabolism
  • Fucose / chemistry*
  • Fucose / metabolism
  • Humans
  • Lectins / chemistry*
  • Lectins / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Quaternary
  • Sequence Alignment


  • Bacterial Proteins
  • Blood Group Antigens
  • Epitopes
  • Lectins
  • Fucose