Structure of the reovirus membrane-penetration protein, μ1, in a complex with its protector protein, σ3

Susanne Liemann, Kartik Chandran, Timothy S. Baker, Max L. Nibert, Stephen C. Harrison

Research output: Contribution to journalArticle

166 Citations (Scopus)

Abstract

Cell entry by nonenveloped animal viruses requires membrane penetration without membrane fusion. The reovirus penetration agent is the outer-capsid protein, μ1. The structure of μ1, complexed with its "protector" protein, σ3, and the fit of this μ13σ33 heterohexameric complex into the cryoEM image of an intact virion, reveal molecular events essential for viral penetration. Autolytic cleavage divides μ1 into myristoylated μ1N and μ1C. A long hydrophobic pocket can receive the myristoyl group. Dissociation of μ1N, linked to a major conformational change of the entire μ1 trimer, must precede myristoyl-group insertion into the cellular membrane. A myristoyl switch, coupling exposure of the fatty acid chain, autolytic cleavage of μ1N, and long-range molecular rearrangement of μ1C, thus appears to be part of the penetration mechanism.

Original languageEnglish (US)
Pages (from-to)283-295
Number of pages13
JournalCell
Volume108
Issue number2
DOIs
StatePublished - Jan 25 2002
Externally publishedYes

Fingerprint

Membrane Proteins
Membranes
Membrane Fusion
Capsid Proteins
Virion
Proteins
Fatty Acids
Viruses
Animals
Fusion reactions
Switches

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Cite this

Structure of the reovirus membrane-penetration protein, μ1, in a complex with its protector protein, σ3. / Liemann, Susanne; Chandran, Kartik; Baker, Timothy S.; Nibert, Max L.; Harrison, Stephen C.

In: Cell, Vol. 108, No. 2, 25.01.2002, p. 283-295.

Research output: Contribution to journalArticle

Liemann, Susanne ; Chandran, Kartik ; Baker, Timothy S. ; Nibert, Max L. ; Harrison, Stephen C. / Structure of the reovirus membrane-penetration protein, μ1, in a complex with its protector protein, σ3. In: Cell. 2002 ; Vol. 108, No. 2. pp. 283-295.
@article{adb0e4dfb1b641e7b1cb6ea061a282b5,
title = "Structure of the reovirus membrane-penetration protein, μ1, in a complex with its protector protein, σ3",
abstract = "Cell entry by nonenveloped animal viruses requires membrane penetration without membrane fusion. The reovirus penetration agent is the outer-capsid protein, μ1. The structure of μ1, complexed with its {"}protector{"} protein, σ3, and the fit of this μ13σ33 heterohexameric complex into the cryoEM image of an intact virion, reveal molecular events essential for viral penetration. Autolytic cleavage divides μ1 into myristoylated μ1N and μ1C. A long hydrophobic pocket can receive the myristoyl group. Dissociation of μ1N, linked to a major conformational change of the entire μ1 trimer, must precede myristoyl-group insertion into the cellular membrane. A myristoyl switch, coupling exposure of the fatty acid chain, autolytic cleavage of μ1N, and long-range molecular rearrangement of μ1C, thus appears to be part of the penetration mechanism.",
author = "Susanne Liemann and Kartik Chandran and Baker, {Timothy S.} and Nibert, {Max L.} and Harrison, {Stephen C.}",
year = "2002",
month = "1",
day = "25",
doi = "10.1016/S0092-8674(02)00612-8",
language = "English (US)",
volume = "108",
pages = "283--295",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "2",

}

TY - JOUR

T1 - Structure of the reovirus membrane-penetration protein, μ1, in a complex with its protector protein, σ3

AU - Liemann, Susanne

AU - Chandran, Kartik

AU - Baker, Timothy S.

AU - Nibert, Max L.

AU - Harrison, Stephen C.

PY - 2002/1/25

Y1 - 2002/1/25

N2 - Cell entry by nonenveloped animal viruses requires membrane penetration without membrane fusion. The reovirus penetration agent is the outer-capsid protein, μ1. The structure of μ1, complexed with its "protector" protein, σ3, and the fit of this μ13σ33 heterohexameric complex into the cryoEM image of an intact virion, reveal molecular events essential for viral penetration. Autolytic cleavage divides μ1 into myristoylated μ1N and μ1C. A long hydrophobic pocket can receive the myristoyl group. Dissociation of μ1N, linked to a major conformational change of the entire μ1 trimer, must precede myristoyl-group insertion into the cellular membrane. A myristoyl switch, coupling exposure of the fatty acid chain, autolytic cleavage of μ1N, and long-range molecular rearrangement of μ1C, thus appears to be part of the penetration mechanism.

AB - Cell entry by nonenveloped animal viruses requires membrane penetration without membrane fusion. The reovirus penetration agent is the outer-capsid protein, μ1. The structure of μ1, complexed with its "protector" protein, σ3, and the fit of this μ13σ33 heterohexameric complex into the cryoEM image of an intact virion, reveal molecular events essential for viral penetration. Autolytic cleavage divides μ1 into myristoylated μ1N and μ1C. A long hydrophobic pocket can receive the myristoyl group. Dissociation of μ1N, linked to a major conformational change of the entire μ1 trimer, must precede myristoyl-group insertion into the cellular membrane. A myristoyl switch, coupling exposure of the fatty acid chain, autolytic cleavage of μ1N, and long-range molecular rearrangement of μ1C, thus appears to be part of the penetration mechanism.

UR - http://www.scopus.com/inward/record.url?scp=0037169362&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037169362&partnerID=8YFLogxK

U2 - 10.1016/S0092-8674(02)00612-8

DO - 10.1016/S0092-8674(02)00612-8

M3 - Article

VL - 108

SP - 283

EP - 295

JO - Cell

JF - Cell

SN - 0092-8674

IS - 2

ER -