Phage pierces the host cell membrane with the iron-loaded spike

Christopher Browning, Mikhail M. Shneider, Valorie D. Bowman, David Schwarzer, Petr Leiman

Research output: Contribution to journalArticle

44 Citations (Scopus)

Abstract

Bacteriophages with contractile tails and the bacterial type VI secretion system have been proposed to use a special protein to create an opening in the host cell membrane during infection. These proteins have a modular architecture but invariably contain an oligonucleotide/oligosaccharide-binding (OB-fold) domain and a long β-helical C-terminal domain, which initiates the contact with the host cell membrane. Using X-ray crystallography and electron microscopy, we report the atomic structure of the membrane-piercing proteins from bacteriophages P2 and 92 and identify the residues that constitute the membrane-attacking apex. Both proteins form compact spikes with a ∼10 diameter tip that is stabilized by a centrally positioned iron ion bound by six histidine residues. The accumulated data strongly suggest that, in the process of membrane penetration, the spikes are translocated through the lipid bilayer without undergoing major unfolding.

Original languageEnglish (US)
Pages (from-to)326-339
Number of pages14
JournalStructure
Volume20
Issue number2
DOIs
StatePublished - Feb 8 2012
Externally publishedYes

Fingerprint

Bacteriophages
Iron
Cell Membrane
Bacteriophage P2
Proteins
Membranes
X Ray Crystallography
Lipid Bilayers
Oligosaccharides
Histidine
Oligonucleotides
Electron Microscopy
Membrane Proteins
Ions
Infection
Type VI Secretion Systems

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

Cite this

Browning, C., Shneider, M. M., Bowman, V. D., Schwarzer, D., & Leiman, P. (2012). Phage pierces the host cell membrane with the iron-loaded spike. Structure, 20(2), 326-339. https://doi.org/10.1016/j.str.2011.12.009

Phage pierces the host cell membrane with the iron-loaded spike. / Browning, Christopher; Shneider, Mikhail M.; Bowman, Valorie D.; Schwarzer, David; Leiman, Petr.

In: Structure, Vol. 20, No. 2, 08.02.2012, p. 326-339.

Research output: Contribution to journalArticle

Browning, C, Shneider, MM, Bowman, VD, Schwarzer, D & Leiman, P 2012, 'Phage pierces the host cell membrane with the iron-loaded spike', Structure, vol. 20, no. 2, pp. 326-339. https://doi.org/10.1016/j.str.2011.12.009
Browning, Christopher ; Shneider, Mikhail M. ; Bowman, Valorie D. ; Schwarzer, David ; Leiman, Petr. / Phage pierces the host cell membrane with the iron-loaded spike. In: Structure. 2012 ; Vol. 20, No. 2. pp. 326-339.
@article{f5853768d1144b6f94c98ffa28fcf70c,
title = "Phage pierces the host cell membrane with the iron-loaded spike",
abstract = "Bacteriophages with contractile tails and the bacterial type VI secretion system have been proposed to use a special protein to create an opening in the host cell membrane during infection. These proteins have a modular architecture but invariably contain an oligonucleotide/oligosaccharide-binding (OB-fold) domain and a long β-helical C-terminal domain, which initiates the contact with the host cell membrane. Using X-ray crystallography and electron microscopy, we report the atomic structure of the membrane-piercing proteins from bacteriophages P2 and 92 and identify the residues that constitute the membrane-attacking apex. Both proteins form compact spikes with a ∼10 diameter tip that is stabilized by a centrally positioned iron ion bound by six histidine residues. The accumulated data strongly suggest that, in the process of membrane penetration, the spikes are translocated through the lipid bilayer without undergoing major unfolding.",
author = "Christopher Browning and Shneider, {Mikhail M.} and Bowman, {Valorie D.} and David Schwarzer and Petr Leiman",
year = "2012",
month = "2",
day = "8",
doi = "10.1016/j.str.2011.12.009",
language = "English (US)",
volume = "20",
pages = "326--339",
journal = "Structure with Folding & design",
issn = "0969-2126",
publisher = "Cell Press",
number = "2",

}

TY - JOUR

T1 - Phage pierces the host cell membrane with the iron-loaded spike

AU - Browning, Christopher

AU - Shneider, Mikhail M.

AU - Bowman, Valorie D.

AU - Schwarzer, David

AU - Leiman, Petr

PY - 2012/2/8

Y1 - 2012/2/8

N2 - Bacteriophages with contractile tails and the bacterial type VI secretion system have been proposed to use a special protein to create an opening in the host cell membrane during infection. These proteins have a modular architecture but invariably contain an oligonucleotide/oligosaccharide-binding (OB-fold) domain and a long β-helical C-terminal domain, which initiates the contact with the host cell membrane. Using X-ray crystallography and electron microscopy, we report the atomic structure of the membrane-piercing proteins from bacteriophages P2 and 92 and identify the residues that constitute the membrane-attacking apex. Both proteins form compact spikes with a ∼10 diameter tip that is stabilized by a centrally positioned iron ion bound by six histidine residues. The accumulated data strongly suggest that, in the process of membrane penetration, the spikes are translocated through the lipid bilayer without undergoing major unfolding.

AB - Bacteriophages with contractile tails and the bacterial type VI secretion system have been proposed to use a special protein to create an opening in the host cell membrane during infection. These proteins have a modular architecture but invariably contain an oligonucleotide/oligosaccharide-binding (OB-fold) domain and a long β-helical C-terminal domain, which initiates the contact with the host cell membrane. Using X-ray crystallography and electron microscopy, we report the atomic structure of the membrane-piercing proteins from bacteriophages P2 and 92 and identify the residues that constitute the membrane-attacking apex. Both proteins form compact spikes with a ∼10 diameter tip that is stabilized by a centrally positioned iron ion bound by six histidine residues. The accumulated data strongly suggest that, in the process of membrane penetration, the spikes are translocated through the lipid bilayer without undergoing major unfolding.

UR - http://www.scopus.com/inward/record.url?scp=84856753664&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84856753664&partnerID=8YFLogxK

U2 - 10.1016/j.str.2011.12.009

DO - 10.1016/j.str.2011.12.009

M3 - Article

VL - 20

SP - 326

EP - 339

JO - Structure with Folding & design

JF - Structure with Folding & design

SN - 0969-2126

IS - 2

ER -