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Structure and Immune Recognition of the HIV Glycan Shield.
Annual Review of Biophysics ( IF 12.4 ) Pub Date : 2018-03-29 , DOI: 10.1146/annurev-biophys-060414-034156
Max Crispin 1 , Andrew B Ward 2 , Ian A Wilson 2, 3
Affiliation  

Vaccine design efforts against the human immunodeficiency virus (HIV) have been greatly stimulated by the observation that many infected patients eventually develop highly potent broadly neutralizing antibodies (bnAbs). Importantly, these bnAbs have evolved to recognize not only the two protein components of the viral envelope protein (Env) but also the numerous glycans that form a protective barrier on the Env protein. Because Env is heavily glycosylated compared to host glycoproteins, the glycans have become targets for the antibody response. Therefore, considerable efforts have been made in developing and validating biophysical methods to elucidate the complex structure of the Env-spike glycoprotein, with its combination of glycan and protein epitopes. We illustrate here how the application of robust biophysical methods has transformed our understanding of the structure and function of the HIV Env spike and stimulated innovation in vaccine design strategies that takes into account the essential glycan components.

中文翻译:

HIV聚糖屏蔽的结构和免疫识别。

观察到许多受感染的患者最终会产生高度有效的广泛中和抗体(bnAbs),这一发现极大地刺激了针对人类免疫缺陷病毒(HIV)的疫苗设计工作。重要的是,这些bnAb不仅可以识别病毒包膜蛋白(Env)的两个蛋白成分,而且可以识别对Env蛋白形成保护性屏障的众多聚糖。由于与宿主糖蛋白相比,Env的糖基化程度很高,因此聚糖已成为抗体反应的靶标。因此,在开发和验证生物物理学方法方面已经做出了相当大的努力,以阐明Env-spike糖蛋白及其聚糖和蛋白表位的组合的复杂结构。
更新日期:2018-05-24
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