甘露糖
凝集素
木菠萝素
聚糖
甘露聚糖结合凝集素
生物化学
甘露糖受体
生物
半乳糖
化学
糖蛋白
体外
巨噬细胞
作者
Annick Barre,Yves Bourne,Els J. M. Van Damme,Willy J. Peumans,Pierre Rougé
出处
期刊:Biochimie
[Elsevier]
日期:2001-07-01
卷期号:83 (7): 645-651
被引量:161
标识
DOI:10.1016/s0300-9084(01)01315-3
摘要
Mannose-specific lectins are widely distributed in higher plants and are believed to play a role in recognition of high-mannose type glycans of foreign micro-organisms or plant predators. Structural studies have demonstrated that the mannose-binding specificity of lectins is mediated by distinct structural scaffolds. The mannose/glucose-specific legume (e.g., Con A, pea lectin) exhibit the canonical twelve-stranded beta-sandwich structure. In contrast to legume lectins that interact with both mannose and glucose, the monocot mannose-binding lectins (e.g., the Galanthus nivalis agglutinin or GNA from bulbs) react exclusively with mannose and mannose-containing N-glycans. These lectins possess a beta-prism structure. More recently, an increasing number of mannose-specific lectins structurally related to jacalin (e.g., the lectins from the Jerusalem artichoke, banana or rice), which also exhibit a beta-prism organization, were characterized. Jacalin itself was re-defined as a polyspecific lectin which, in addition to galactose, also interacts with mannose and mannose-containing glycans. Finally the B-chain of the type II RIP of iris, which has the same beta-prism structure as all other members of the ricin-B family, interacts specifically with mannose and galactose. This structural diversity associated with the specific recognition of high-mannose type glycans highlights the importance of mannose-specific lectins as recognition molecules in higher plants.
科研通智能强力驱动
Strongly Powered by AbleSci AI