PUTATIVE RECEPTOR-BINDING SITES ON ALPHAVIRUSES AS VISUALIZED BY CRYOELECTRON MICROSCOPY

被引：118

作者：

SMITH, TJ

CHENG, RH

OLSON, NH

PETERSON, P

CHASE, E

KUHN, RJ

BAKER, TS

机构：

[1] Department of Biological Sciences, Purdue University, West Lafayette

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1995年 / 92卷 / 23期

关键词：

ANTIBODIES; NEUTRALIZATION; SINDBIS VIRUS; ROSS RIVER VIRUS;

D O I：

10.1073/pnas.92.23.10648

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：10648 / 10652

页数：5

共 49 条

[1] PROTEIN-PROTEIN INTERACTIONS IN AN ALPHAVIRUS MEMBRANE [J].