. "3"^^ . "\u0160ul\u00E1k, Ond\u0159ej" . "US - Spojen\u00E9 st\u00E1ty americk\u00E9" . "RIV/00216224:14310/10:00057175!RIV13-GA0-14310___" . "Delia, Monia" . "A TNF-like Trimeric Lectin Domain from Burkholderia cenocepacia with Specificity for Fucosylated Human Histo-Blood Group Antigens" . "000273859700010" . . . "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."@en . . . "Delia, Monia" . . "14310" . "0969-2126" . "10.1016/j.str.2009.10.021" . "lectin; Burkholderia cenocepacia; pathogen; TNF"@en . "A TNF-like Trimeric Lectin Domain from Burkholderia cenocepacia with Specificity for Fucosylated Human Histo-Blood Group Antigens"@en . "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." . "Wimmerov\u00E1, Michaela" . . "Cioci, Gianluca" . "Lahmann, Martina" . . "Imberty, Anne" . "RIV/00216224:14310/10:00057175" . . "[9EB39E2574DA]" . "A TNF-like Trimeric Lectin Domain from Burkholderia cenocepacia with Specificity for Fucosylated Human Histo-Blood Group Antigens" . . . "245037" . "18" . . . . . . "P(GA303/09/1168), P(GD301/09/H004), P(LC06030), S, Z(MSM0021622413)" . . "7"^^ . "14"^^ . . . "Structure" . . "1" . . . "Varrot, Annabelle" . "A TNF-like Trimeric Lectin Domain from Burkholderia cenocepacia with Specificity for Fucosylated Human Histo-Blood Group Antigens"@en .