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

doi:10.1073/pnas.92.23.10648

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 journal › Article › peer-review

118 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 language	English (US)
Pages (from-to)	10648-10652
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	92
Issue number	23
DOIs	https://doi.org/10.1073/pnas.92.23.10648
State	Published - Nov 7 1995
Externally published	Yes

Keywords

Ross River virus
Sindbis virus
antibodies
neutralization

ASJC Scopus subject areas

General

Access to Document

10.1073/pnas.92.23.10648

Cite this

@article{88591e24778841a6922c08b1f7c5a878,

title = "Putative receptor binding sites on alphaviruses as visualized by cryoelectron microscopy",

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.",

keywords = "Ross River virus, Sindbis virus, antibodies, neutralization",

author = "Smith, {Thomas J.} and Cheng, {R. Holland} and Olson, {Norman H.} and Peter Peterson and Elaine Chase and Kuhn, {Richard J.} and Baker, {Timothy S.}",

year = "1995",

month = nov,

day = "7",

doi = "10.1073/pnas.92.23.10648",

language = "English (US)",

volume = "92",

pages = "10648--10652",

journal = "Proceedings of the National Academy of Sciences of the United States of America",

issn = "0027-8424",

publisher = "National Academy of Sciences",

number = "23",

}

TY - JOUR

T1 - Putative receptor binding sites on alphaviruses as visualized by cryoelectron microscopy

AU - Smith, Thomas J.

AU - Cheng, R. Holland

AU - Olson, Norman H.

AU - Peterson, Peter

AU - Chase, Elaine

AU - Kuhn, Richard J.

AU - Baker, Timothy S.

PY - 1995/11/7

Y1 - 1995/11/7

N2 - 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.

AB - 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.

KW - Ross River virus

KW - Sindbis virus

KW - antibodies

KW - neutralization

UR - http://www.scopus.com/inward/record.url?scp=0028804905&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028804905&partnerID=8YFLogxK

U2 - 10.1073/pnas.92.23.10648

DO - 10.1073/pnas.92.23.10648

M3 - Article

C2 - 7479858

AN - SCOPUS:0028804905

SN - 0027-8424

VL - 92

SP - 10648

EP - 10652

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

IS - 23

ER -

Putative receptor binding sites on alphaviruses as visualized by cryoelectron microscopy

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this