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

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

Research output: Contribution to journalArticlepeer-review

56 Scopus citations


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
Issue number2
StatePublished - Feb 8 2012
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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