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  Incomplete pneumolysin oligomers form membrane pores

Sonnen, A.-F.-P., Plitzko, J. M., & Gilbert, R. J. C. (2014). Incomplete pneumolysin oligomers form membrane pores. OPEN BIOLOGY, 4(4): [4:140044]. doi:10.1098/rsob.140044.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-CF32-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-CF35-5
Genre: Journal Article

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 Creators:
Sonnen, Andreas F.-P.1, Author              
Plitzko, Jürgen M.1, Author              
Gilbert, Robert J. C.2, Author
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1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2external, ou_persistent22              

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Free keywords: CHOLESTEROL-DEPENDENT CYTOLYSINS; BACTERIAL TOXIN PNEUMOLYSIN; PROTEIN TOXIN; PERFRINGOLYSIN-O; DIVALENT-CATIONS; DAMAGE MEMBRANES; LIPID-MEMBRANES; ATTACK COMPLEX; STREPTOLYSIN-O; TELL USpneumolysin; pore formation; cryo-electron tomography; proteolipid pore; toroidal pore;
 Abstract: Pneumolysin is a member of the cholesterol-dependent cytolysin (CDC) family of pore-forming proteins that are produced as water-soluble monomers or dimers, bind to target membranes and oligomerize into large ring-shaped assemblies comprising approximately 40 subunits and approximately 30 nm across. This pre-pore assembly then refolds to punch a large hole in the lipid bilayer. However, in addition to forming large pores, pneumolysin and other CDCs formsmaller lesions characterized by low electrical conductance. Owing to the observation of arc-like (rather than full-ring) oligomers by electron microscopy, it has been hypothesized that smaller oligomers explain smaller functional pores. To investigate whether this is the case, we performed cryo-electron tomography of pneumolysin oligomers on model lipid membranes. We then used sub-tomogram classification and averaging to determine representative membrane-bound low-resolution structures and identified pre-pores versus pores by the presence of membrane within the oligomeric curve. We found pre-pore and pore forms of both complete (ring) and incomplete (arc) oligomers and conclude that arc-shaped oligomeric assemblies of pneumolysin can form pores. As the CDCs are evolutionarily related to the membrane attack complex/perforin family of proteins, which also form variably sized pores, our findings are of relevance to that class of proteins as well.

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Language(s): eng - English
 Dates: 2014-04
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: ISI: 000335813800009
DOI: 10.1098/rsob.140044
 Degree: -

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Title: OPEN BIOLOGY
Source Genre: Journal
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Publ. Info: 6-9 CARLTON HOUSE TERRACE, LONDON SW1Y 5AG, ENGLAND : ROYAL SOC
Pages: - Volume / Issue: 4 (4) Sequence Number: [4:140044] Start / End Page: - Identifier: ISSN: 2046-2441