期刊
ELIFE
卷 3, 期 -, 页码 -出版社
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.04247
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资金
- Biotechnology and Biological Sciences Research Council [BB/G011729/1, BB/J005932/1, BB/J006254, BB/K01692X/1]
- European Research Council [294408]
- Leverhulme Trust [RPG-2012-519]
- Biotechnology and Biological Sciences Research Council [BB/J005932/1, BB/G011729/1, BB/J006254/1, BB/K01692X/1] Funding Source: researchfish
- BBSRC [BB/G011729/1, BB/J005932/1, BB/J006254/1, BB/K01692X/1] Funding Source: UKRI
- European Research Council (ERC) [294408] Funding Source: European Research Council (ERC)
Membrane attack complex/perforin/cholesterol-dependent cytolysin (MACPF/CDC) proteins constitute a major superfamily of pore-forming proteins that act as bacterial virulence factors and effectors in immune defence. Upon binding to the membrane, they convert from the soluble monomeric form to oligomeric, membrane-inserted pores. Using real-time atomic force microscopy (AFM), electron microscopy (EM), and atomic structure fitting, we have mapped the structure and assembly pathways of a bacterial CDC in unprecedented detail and accuracy, focussing on suilysin from Streptococcus suis. We show that suilysin assembly is a noncooperative process that is terminated before the protein inserts into the membrane. The resulting ring-shaped pores and kinetically trapped arc-shaped assemblies are all seen to perforate the membrane, as also visible by the ejection of its lipids. Membrane insertion requires a concerted conformational change of the monomeric subunits, with a marked expansion in pore diameter due to large changes in subunit structure and packing.
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