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首页> 外文期刊>Acta crystallographica. Section D, Structural biology. >X‐ray and EM structures of a natively glycosylated HIV‐1 envelope trimer
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X‐ray and EM structures of a natively glycosylated HIV‐1 envelope trimer

机译：X射线和EM本地糖化的结构艾滋病毒检测1信封三聚物

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摘要

The structural and biochemical characterization of broadly neutralizing anti‐HIV‐1 antibodies (bNAbs) has been essential in guiding the design of potential vaccines to prevent infection by HIV‐1. While these studies have revealed critical mechanisms by which bNAbs recognize and/or accommodate N‐glycans on the trimeric envelope glycoprotein (Env), they have been limited to the visualization of high‐mannose glycan forms only, since heterogeneity introduced from the presence of complex glycans makes it difficult to obtain high‐resolution structures. 3.5 and 3.9?? resolution crystal structures of the HIV‐1 Env trimer with fully processed and native glycosylation were solved, revealing a glycan shield of high‐mannose and complex‐type N‐glycans that were used to define the complete epitopes of two bNAbs. Here, the refinement of the N‐glycans in the crystal structures is discussed and comparisons are made with glycan densities in glycosylated Env structures derived by single‐particle cryo‐electron microscopy.
机译：的结构和生化特征广泛的中和抗艾滋病毒检测1抗体(bnab)已经基本指导设计潜在的疫苗来预防感染艾滋病毒检测——1。bnab识别和/或机制适应N量聚糖三聚物的信封糖蛋白(Env),他们一直局限于的可视化高甘露糖多糖形式,自从引进存在异质性复杂的聚糖很难获得高分辨率的结构。艾滋病毒检测的分辨率晶体结构1 Env三聚物完全处理和本地糖基化是解决,揭示多糖盾的高甘露糖和复杂类型N量聚糖用于定义完整的抗原表位两个bnab。在讨论和晶体结构比较是由多糖密度导出了糖化Env结构单量粒子低温电子显微镜。

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