Imberty Anne, Varrot Annabelle
CERMAV-CNRS (UPR5301, affiliated with Université Joseph Fourier and belonging to ICMG), BP53, F38041 Grenoble Cedex 9, France.
Curr Opin Struct Biol. 2008 Oct;18(5):567-76. doi: 10.1016/j.sbi.2008.08.001. Epub 2008 Oct 1.
Infection by pathogens is generally initiated by the specific recognition of host epithelia surfaces and subsequent adhesion is essential for invasion. In their infection strategy, microorganisms often use sugar-binding proteins, that is lectins and adhesins, to recognize and bind to host glycoconjugates where sialylated and fucosylated oligosaccharides are the major targets. The lectin/glycoconjugate interactions are characterized by their high specificity and most of the time by multivalency to generate higher affinity of binding. Recent crystal structures of viral, bacterial, and parasite receptors in complex with human histo-blood group epitopes or sialylated derivatives reveal new folds and novel sugar-binding modes. They illustrate the tight specificity between tissue glycosylation and lectins.
病原体感染通常始于对宿主上皮表面的特异性识别，随后的黏附对于入侵至关重要。在其感染策略中，微生物常常利用糖结合蛋白，即凝集素和黏附素，来识别并结合宿主糖缀合物，其中唾液酸化和岩藻糖基化寡糖是主要靶点。凝集素/糖缀合物相互作用的特点是具有高度特异性，并且大多数情况下具有多价性以产生更高的结合亲和力。近期病毒、细菌和寄生虫受体与人类组织血型抗原表位或唾液酸化衍生物复合物的晶体结构揭示了新的折叠方式和新颖的糖结合模式。它们阐明了组织糖基化与凝集素之间的紧密特异性。
