Norovirus and histo-blood group antigens: Demonstration of a wide spectrum of strain specificities and classification of two major binding groups among multiple binding patterns
Norovirus and histo-blood group antigens: Demonstration of a wide spectrum of strain specificities and classification of two major binding groups among multiple binding patterns
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DOI：
10.1128/jvi.79.11.6714-6722.2005
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发表时间：
2005-06-01
影响因子：
5.4
通讯作者：
Xi, J
中科院分区：
文献类型：
--
作者：
Huang, PW;Farkas, T;Xi, J
诺如病毒是引起急性胃肠炎的一个重要原因，已发现它能识别人类组织血型抗原(HBGA)作为受体。我们在上一份报告中描述了四种菌株与HBGA的特异结合模式。在这项研究中，我们基于14种诺如病毒的研究将结合模式扩展到7种。基于低聚糖的分析揭示了基于唾液的分析没有检测到的其他表位。根据它们与人HBGA的三个主要表位(A/B、H和Lewis)的相互作用，这七种模式被分为两类：A/B结合组和Lewis结合组。A/B结合组中的菌株识别A和/或B和H抗原，但不识别Lewis抗原，而Lewis结合组中的菌株仅对Lewis和/或H抗原反应。这一分类也导致了诺沃克病毒/HBGA相互作用的模型。系统发育分析表明，具有相同或密切相关结合模式的毒株倾向于聚类，但两个结合群中的毒株均可在I和II基因组中找到。我们的结果表明，诺如病毒具有广泛的宿主范围，人类HBGA在诺如病毒的进化中发挥着重要作用。人类HBGA系统的高度多态，涉及多个表位，以及诺如病毒VLP和HBGA之间典型的蛋白质/碳水化合物相互作用，为病毒与配体结合的多样性提供了解释。
Noroviruses, an important cause of acute gastroenteritis, have been found to recognize human histo-blood group antigens (HBGAs) as receptors. Four strain-specific binding patterns to HBGAs have been described in our previous report. In this study, we have extended the binding patterns to seven based on 14 noroviruses examined. The oligosaccharide-based assays revealed additional epitopes that were not detected by the saliva-based assays. The seven patterns have been classified into two groups according to their interactions with three major epitopes (A/B, H, and Lewis) of human HBGAs: the A/B-binding group and the Lewis-binding group. Strains in the A/B binding group recognize the A and/or B and H antigens, but not the Lewis antigens, while strains in the Lewis-binding group react only to the Lewis and/or H antigens. This classification also resulted in a model of the norovirus/HBGA interaction. Phylogenetic analyses showed that strains with identical or closely related binding patterns tend to be clustered, but strains in both binding group can be found in both genogroups I and II. Our results suggest that noroviruses have a wide spectrum of host range and that human HBGAs play an important role in norovirus evolution. The high polymorphism of the human HBGA system, the involvement of multiple epitopes, and the typical protein/carbohydrate interaction between norovirus VLPs and HBGAs provide an explanation for the virus-ligand binding diversities.