Journal
NATURE NANOTECHNOLOGY
Volume 12, Issue 5, Pages 467-473Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NNANO.2016.303
Keywords
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Funding
- BBSRC [BB/J005932/1, BB/J006254/1, BB/N015487/1]
- ERC [294408]
- Wellcome Trust [079605/2/06/02]
- NHMRC Fellowship [1059126, 1062706, 1013667]
- Sackler Foundation
- Biotechnology and Biological Sciences Research Council [BB/J006254/1, BB/J005932/1, BB/N015487/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/M028100/1] Funding Source: researchfish
- National Health and Medical Research Council of Australia [1062706, 1059126] Funding Source: NHMRC
- European Research Council (ERC) [294408] Funding Source: European Research Council (ERC)
- BBSRC [BB/J005932/1, BB/J006254/1, BB/N015487/1] Funding Source: UKRI
- EPSRC [EP/M028100/1] Funding Source: UKRI
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Perforin is a key protein of the vertebrate immune system. Secreted by cytotoxic lymphocytes as soluble monomers, perforin can self-assemble into oligomeric pores of 10-20 nm inner diameter in the membranes of virus-infected and cancerous cells. These large pores facilitate the entry of pro-apoptotic granzymes, thereby rapidly killing the target cell. To elucidate the pathways of perforin pore assembly, we carried out real-time atomic force microscopy and electron microscopy studies. Our experiments reveal that the pore assembly proceeds via a membrane-bound prepore intermediate state, typically consisting of up to approximately eight loosely but irreversibly assembled monomeric subunits. These short oligomers convert to more closely packed membrane nanopore assemblies, which can subsequently recruit additional prepore oligomers to grow the pore size.
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