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首页> 外文会议>International Conference on Innovative Material Science and Technology >Functional evaluation of bacterial surface displayed P domain from human norovirus capsid proteins
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Functional evaluation of bacterial surface displayed P domain from human norovirus capsid proteins

机译：细菌表面的功能评估显示来自人诺维病毒衣壳蛋白的P域

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Human noroviruses (HuNoVs) are the major cause to acute nonbacterial gastroenteritis outbreaks. The receptors of HuNoVs are difficult to identify because HuNoVs cannot be easily cultivated in vitro and they lack effective animal models. To develop an effective method for mining functional viral receptors, engineering Escherichia coli were constructed to display P domain of capsid protein of HuNoVs (GI.1 or GII.4) on the cell surface, using the N-terminal of the ice nucleation protein (InaQN). In this study, membrane protein-porcine gastric mucin binding ELISA methods were employed to confirm the surface display efficiency. The receptor binding capacity of InaQN-P (GI.1 or GII.4) fusion proteins on the bacterial surface was evaluated through whole-cell fluorescence immunoassay with saliva-based histo-blood group antigens. Results revealed remarkable characteristic of antigenicity and receptor binding properties. Therefore, this bacterial surface display system should be considered as a candidate to mine and investigate HuNoV receptors in vivo or in vitro.
机译：人类诺罗病毒（Hunovs）是急性无细菌性胃肠炎爆发的主要原因。洪水的受体难以识别，因为亨术族不能在体外容易培养，并且它们缺乏有效的动物模型。为了开发有效的采矿功能性病毒受体方法，使用冰核蛋白的N-末端（in-Tember）构建工程大肠杆菌以显示在细胞表面上的亨西氏囊蛋白（Gi.1或Gii.4）的P领域（ inaaqn）。在该研究中，采用膜蛋白 - 猪胃粘蛋白结合ELISA方法来证实表面显示效率。该受体在细菌表面结合InaQN-P（GI.1或GII.4）融合蛋白的能力是通过全细胞荧光免疫评估了基于唾液的组织血型抗原。结果揭示了抗原性和受体结合特性的显着特征。因此，这种细菌表面显示系统应被认为是矿山的候选者，并在体内或体外调查Hunov受体。

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