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通过冷冻电子显微镜观察到的甲病毒上的假定受体结合位点。

Putative receptor binding sites on alphaviruses as visualized by cryoelectron microscopy.

作者信息

Smith T J, Cheng R H, Olson N H, Peterson P, Chase E, Kuhn R J, Baker T S

机构信息

Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-1392, USA.

出版信息

Proc Natl Acad Sci U S A. 1995 Nov 7;92(23):10648-52. doi: 10.1073/pnas.92.23.10648.

Abstract

The structures of Sindbis virus and Ross River virus complexed with Fab fragments from monoclonal antibodies have been determined from cryoelectron micrographs. Both antibodies chosen for this study bind to regions of the virions that have been implicated in cell-receptor recognition and recognize epitopes on the E2 glycoprotein. The two structures show that the Fab fragments bind to the outermost tip of the trimeric envelope spike protein. Hence, the same region of both the Sindbis virus and Ross River virus envelope spike is composed of E2 and is involved in recognition of the cellular receptor.

摘要

已通过冷冻电子显微镜确定了与单克隆抗体的Fab片段复合的辛德毕斯病毒和罗斯河病毒的结构。本研究选择的两种抗体均与病毒粒子中与细胞受体识别有关的区域结合,并识别E2糖蛋白上的表位。这两种结构表明,Fab片段与三聚体包膜刺突蛋白的最外端结合。因此,辛德毕斯病毒和罗斯河病毒包膜刺突的相同区域均由E2组成,并参与细胞受体的识别。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/064e/40669/f4851d67b0f7/pnas01501-0215-a.jpg

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