A TNF-like Trimeric Lectin Domain from Burkholdeda cenocepacia with Specificity for Fucosylated Human Histo-Blood Group Antigens
A TNF-like Trimeric Lectin Domain from Burkholdeda cenocepacia with Specificity for Fucosylated Human Histo-Blood Group Antigens
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DOI：
10.1016/j.str.2009.10.021
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发表时间：
2010-01-13
期刊：
影响因子：
5.7
通讯作者：
Wimmerova, Michaela
中科院分区：
文献类型：
--
作者：
Sulak, Ondrej;Cioci, Gianluca;Wimmerova, Michaela
机会性病原体新洋葱伯克霍尔德杆菌表达多种可溶性凝集素，其中包括 BC2L-C。该凝集素具有两个结构域：一个与最近描述的钙依赖性甘露糖结合凝集素 BC2L-A 具有高度序列相似性的 C 端结构域，以及一个由 156 个氨基酸组成的 N 端结构域，与任何已知蛋白质没有相似性。重组 N 端 BC2L-C 结构域是一种新型凝集素，通过聚糖阵列和等温滴定量热法测定，对岩藻糖基化人组织血型表位 H-1 型、Lewis b 和 Lewis Y 具有特异性。以甲基硒岩藻糖苷为配体解析N端BC2L-C结构域的晶体结构。其他分子模型研究合理化了对路易斯表位的偏好。该结构揭示了三聚果冻卷排列，与 TNF 样蛋白和 BciA（炭疽芽孢杆菌的孢子蛋白）具有惊人的相似性，BciA 可能在人类肺部炭疽孢子的生物粘附中发挥重要作用。
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.