Membrane proteins organize a symmetrical virus

Kerstin Forsell, Li Xing, Tatyana Kozlovska, R. Holland Cheng, Henrik Garoff

Research output: Contribution to journalArticle

64 Citations (Scopus)

Abstract

Alphaviruses are enveloped icosahedral viruses that mature by budding at the plasma membrane. According to a prevailing model maturation is driven by binding of membrane protein spikes to a preformed nucleocapsid (NC). The T = 4 geometry of the membrane is thought to be imposed by the NC through one-to-one interactions between spike protomers and capsid proteins (CPs). This model is challenged here by a Semliki Forest virus capsid gene mutant. Its CPs cannot assemble into NCs, or its intermediate structures, due to defective CP-CP interactions. Nevertheless, it can use its horizontal spike-spike interactions on membrane surface and vertical spike-CP interactions to make a particle with correct geometry and protein stoichiometry. Thus, our results highlight the direct role of membrane proteins in organizing the icosahedral conformation of alphaviruses.

Original languageEnglish (US)
Pages (from-to)5081-5091
Number of pages11
JournalEMBO Journal
Volume19
Issue number19
StatePublished - Oct 2 2000
Externally publishedYes

Fingerprint

Capsid Proteins
Viruses
Membrane Proteins
Alphavirus
Nucleocapsid
Semliki forest virus
Virus Release
Membranes
Geometry
Capsid
Protein Subunits
Cell membranes
Stoichiometry
Conformations
Carrier Proteins
Genes
Cell Membrane
Proteins

Keywords

  • Alphavirus
  • Budding
  • Glycoprotein
  • Horizontal interactions

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

Cite this

Forsell, K., Xing, L., Kozlovska, T., Cheng, R. H., & Garoff, H. (2000). Membrane proteins organize a symmetrical virus. EMBO Journal, 19(19), 5081-5091.

Membrane proteins organize a symmetrical virus. / Forsell, Kerstin; Xing, Li; Kozlovska, Tatyana; Cheng, R. Holland; Garoff, Henrik.

In: EMBO Journal, Vol. 19, No. 19, 02.10.2000, p. 5081-5091.

Research output: Contribution to journalArticle

Forsell, K, Xing, L, Kozlovska, T, Cheng, RH & Garoff, H 2000, 'Membrane proteins organize a symmetrical virus', EMBO Journal, vol. 19, no. 19, pp. 5081-5091.
Forsell K, Xing L, Kozlovska T, Cheng RH, Garoff H. Membrane proteins organize a symmetrical virus. EMBO Journal. 2000 Oct 2;19(19):5081-5091.
Forsell, Kerstin ; Xing, Li ; Kozlovska, Tatyana ; Cheng, R. Holland ; Garoff, Henrik. / Membrane proteins organize a symmetrical virus. In: EMBO Journal. 2000 ; Vol. 19, No. 19. pp. 5081-5091.
@article{70a55332771f4b6987b499c3af7a1a8e,
title = "Membrane proteins organize a symmetrical virus",
abstract = "Alphaviruses are enveloped icosahedral viruses that mature by budding at the plasma membrane. According to a prevailing model maturation is driven by binding of membrane protein spikes to a preformed nucleocapsid (NC). The T = 4 geometry of the membrane is thought to be imposed by the NC through one-to-one interactions between spike protomers and capsid proteins (CPs). This model is challenged here by a Semliki Forest virus capsid gene mutant. Its CPs cannot assemble into NCs, or its intermediate structures, due to defective CP-CP interactions. Nevertheless, it can use its horizontal spike-spike interactions on membrane surface and vertical spike-CP interactions to make a particle with correct geometry and protein stoichiometry. Thus, our results highlight the direct role of membrane proteins in organizing the icosahedral conformation of alphaviruses.",
keywords = "Alphavirus, Budding, Glycoprotein, Horizontal interactions",
author = "Kerstin Forsell and Li Xing and Tatyana Kozlovska and Cheng, {R. Holland} and Henrik Garoff",
year = "2000",
month = "10",
day = "2",
language = "English (US)",
volume = "19",
pages = "5081--5091",
journal = "EMBO Journal",
issn = "0261-4189",
publisher = "Nature Publishing Group",
number = "19",

}

TY - JOUR

T1 - Membrane proteins organize a symmetrical virus

AU - Forsell, Kerstin

AU - Xing, Li

AU - Kozlovska, Tatyana

AU - Cheng, R. Holland

AU - Garoff, Henrik

PY - 2000/10/2

Y1 - 2000/10/2

N2 - Alphaviruses are enveloped icosahedral viruses that mature by budding at the plasma membrane. According to a prevailing model maturation is driven by binding of membrane protein spikes to a preformed nucleocapsid (NC). The T = 4 geometry of the membrane is thought to be imposed by the NC through one-to-one interactions between spike protomers and capsid proteins (CPs). This model is challenged here by a Semliki Forest virus capsid gene mutant. Its CPs cannot assemble into NCs, or its intermediate structures, due to defective CP-CP interactions. Nevertheless, it can use its horizontal spike-spike interactions on membrane surface and vertical spike-CP interactions to make a particle with correct geometry and protein stoichiometry. Thus, our results highlight the direct role of membrane proteins in organizing the icosahedral conformation of alphaviruses.

AB - Alphaviruses are enveloped icosahedral viruses that mature by budding at the plasma membrane. According to a prevailing model maturation is driven by binding of membrane protein spikes to a preformed nucleocapsid (NC). The T = 4 geometry of the membrane is thought to be imposed by the NC through one-to-one interactions between spike protomers and capsid proteins (CPs). This model is challenged here by a Semliki Forest virus capsid gene mutant. Its CPs cannot assemble into NCs, or its intermediate structures, due to defective CP-CP interactions. Nevertheless, it can use its horizontal spike-spike interactions on membrane surface and vertical spike-CP interactions to make a particle with correct geometry and protein stoichiometry. Thus, our results highlight the direct role of membrane proteins in organizing the icosahedral conformation of alphaviruses.

KW - Alphavirus

KW - Budding

KW - Glycoprotein

KW - Horizontal interactions

UR - http://www.scopus.com/inward/record.url?scp=0034596852&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034596852&partnerID=8YFLogxK

M3 - Article

C2 - 11013211

AN - SCOPUS:0034596852

VL - 19

SP - 5081

EP - 5091

JO - EMBO Journal

JF - EMBO Journal

SN - 0261-4189

IS - 19

ER -