Nucleocapsid and glycoprotein organization in an enveloped virus

R. Holland Cheng, Richard J. Kuhn, Norman H. Olson, Michael G. Rossmann^Hok-Kin Choi, Thomas Smith, Timothy S. Baker

Research output: Contribution to journalArticle

248 Citations (Scopus)

Abstract

Alphaviruses are a group of icosahedral, positive-strand RNA, enveloped viruses. The membrane bilayer, which surrounds the ∼ 400 Å diameter nucleocapsid, is penetrated by 80 spikes arranged in a T = 4 lattice. Each spike is a trimer of heterodimers consisting of glycoproteins Ell and E2. Cryoelectron microscopy and image reconstruction of Ross River virus showed that the T=4 quaternary structure of the nucleocapsid consists of pentamerand hexamer clusters of the capsid protein, but not dimers, as have been observed in several crystallographic studies. The E1-E2 heterodimers form one-to-one associations with the nucleocapsid monomers across the lipid bilayer. Knowledge of the atomic structure of the capsid protein and our reconstruction allows us to identify capsid-protein residues that interact with the RNA, the glycoproteins, and adjacent capsid-proteins.

Original languageEnglish (US)
Pages (from-to)621-630
Number of pages10
JournalCell
Volume80
Issue number4
DOIs
StatePublished - Feb 24 1995
Externally publishedYes

Fingerprint

Nucleocapsid
Capsid Proteins
Viruses
Glycoproteins
Ross River virus
RNA
Alphavirus
Cryoelectron Microscopy
Lipid bilayers
Computer-Assisted Image Processing
RNA Viruses
Lipid Bilayers
Image reconstruction
Dimers
Microscopic examination
Monomers
Rivers
Membranes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Cell Biology
  • Molecular Biology

Cite this

Holland Cheng, R., Kuhn, R. J., Olson, N. H., Rossmann^Hok-Kin Choi, M. G., Smith, T., & Baker, T. S. (1995). Nucleocapsid and glycoprotein organization in an enveloped virus. Cell, 80(4), 621-630. https://doi.org/10.1016/0092-8674(95)90516-2

Nucleocapsid and glycoprotein organization in an enveloped virus. / Holland Cheng, R.; Kuhn, Richard J.; Olson, Norman H.; Rossmann^Hok-Kin Choi, Michael G.; Smith, Thomas; Baker, Timothy S.

In: Cell, Vol. 80, No. 4, 24.02.1995, p. 621-630.

Research output: Contribution to journalArticle

Holland Cheng, R, Kuhn, RJ, Olson, NH, Rossmann^Hok-Kin Choi, MG, Smith, T & Baker, TS 1995, 'Nucleocapsid and glycoprotein organization in an enveloped virus', Cell, vol. 80, no. 4, pp. 621-630. https://doi.org/10.1016/0092-8674(95)90516-2
Holland Cheng R, Kuhn RJ, Olson NH, Rossmann^Hok-Kin Choi MG, Smith T, Baker TS. Nucleocapsid and glycoprotein organization in an enveloped virus. Cell. 1995 Feb 24;80(4):621-630. https://doi.org/10.1016/0092-8674(95)90516-2
Holland Cheng, R. ; Kuhn, Richard J. ; Olson, Norman H. ; Rossmann^Hok-Kin Choi, Michael G. ; Smith, Thomas ; Baker, Timothy S. / Nucleocapsid and glycoprotein organization in an enveloped virus. In: Cell. 1995 ; Vol. 80, No. 4. pp. 621-630.
@article{7ce37867f013490392c87141696f147d,
title = "Nucleocapsid and glycoprotein organization in an enveloped virus",
abstract = "Alphaviruses are a group of icosahedral, positive-strand RNA, enveloped viruses. The membrane bilayer, which surrounds the ∼ 400 {\AA} diameter nucleocapsid, is penetrated by 80 spikes arranged in a T = 4 lattice. Each spike is a trimer of heterodimers consisting of glycoproteins Ell and E2. Cryoelectron microscopy and image reconstruction of Ross River virus showed that the T=4 quaternary structure of the nucleocapsid consists of pentamerand hexamer clusters of the capsid protein, but not dimers, as have been observed in several crystallographic studies. The E1-E2 heterodimers form one-to-one associations with the nucleocapsid monomers across the lipid bilayer. Knowledge of the atomic structure of the capsid protein and our reconstruction allows us to identify capsid-protein residues that interact with the RNA, the glycoproteins, and adjacent capsid-proteins.",
author = "{Holland Cheng}, R. and Kuhn, {Richard J.} and Olson, {Norman H.} and {Rossmann^Hok-Kin Choi}, {Michael G.} and Thomas Smith and Baker, {Timothy S.}",
year = "1995",
month = "2",
day = "24",
doi = "10.1016/0092-8674(95)90516-2",
language = "English (US)",
volume = "80",
pages = "621--630",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "4",

}

TY - JOUR

T1 - Nucleocapsid and glycoprotein organization in an enveloped virus

AU - Holland Cheng, R.

AU - Kuhn, Richard J.

AU - Olson, Norman H.

AU - Rossmann^Hok-Kin Choi, Michael G.

AU - Smith, Thomas

AU - Baker, Timothy S.

PY - 1995/2/24

Y1 - 1995/2/24

N2 - Alphaviruses are a group of icosahedral, positive-strand RNA, enveloped viruses. The membrane bilayer, which surrounds the ∼ 400 Å diameter nucleocapsid, is penetrated by 80 spikes arranged in a T = 4 lattice. Each spike is a trimer of heterodimers consisting of glycoproteins Ell and E2. Cryoelectron microscopy and image reconstruction of Ross River virus showed that the T=4 quaternary structure of the nucleocapsid consists of pentamerand hexamer clusters of the capsid protein, but not dimers, as have been observed in several crystallographic studies. The E1-E2 heterodimers form one-to-one associations with the nucleocapsid monomers across the lipid bilayer. Knowledge of the atomic structure of the capsid protein and our reconstruction allows us to identify capsid-protein residues that interact with the RNA, the glycoproteins, and adjacent capsid-proteins.

AB - Alphaviruses are a group of icosahedral, positive-strand RNA, enveloped viruses. The membrane bilayer, which surrounds the ∼ 400 Å diameter nucleocapsid, is penetrated by 80 spikes arranged in a T = 4 lattice. Each spike is a trimer of heterodimers consisting of glycoproteins Ell and E2. Cryoelectron microscopy and image reconstruction of Ross River virus showed that the T=4 quaternary structure of the nucleocapsid consists of pentamerand hexamer clusters of the capsid protein, but not dimers, as have been observed in several crystallographic studies. The E1-E2 heterodimers form one-to-one associations with the nucleocapsid monomers across the lipid bilayer. Knowledge of the atomic structure of the capsid protein and our reconstruction allows us to identify capsid-protein residues that interact with the RNA, the glycoproteins, and adjacent capsid-proteins.

UR - http://www.scopus.com/inward/record.url?scp=0028919758&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028919758&partnerID=8YFLogxK

U2 - 10.1016/0092-8674(95)90516-2

DO - 10.1016/0092-8674(95)90516-2

M3 - Article

VL - 80

SP - 621

EP - 630

JO - Cell

JF - Cell

SN - 0092-8674

IS - 4

ER -