Putative receptor binding sites on alphaviruses as visualized by cryoelectron microscopy

Thomas J. Smith, R. Holland Cheng, Norman H. Olson, Peter Peterson, Elaine Chase, Richard J. Kuhn, Timothy S. Baker

Research output: Contribution to journalArticle

96 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)10648-10652
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume92
Issue number23
DOIs
StatePublished - Nov 7 1995

Keywords

  • Ross River virus
  • Sindbis virus
  • antibodies
  • neutralization

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Putative receptor binding sites on alphaviruses as visualized by cryoelectron microscopy'. Together they form a unique fingerprint.

  • Cite this