Effects of MACPF/CDC proteins on lipid membranes
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Cellular and Molecular Life Sciences
REVIEW
Effects of MACPF/CDC proteins on lipid membranes Robert J. C. Gilbert • Miha Mikelj • Mauro Dalla Serra • Christopher J. Froelich Gregor Anderluh
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Received: 29 June 2012 / Revised: 29 August 2012 / Accepted: 30 August 2012 / Published online: 15 September 2012 Ó Springer Basel AG 2012
Abstract Recent work on the MACPF/CDC superfamily of pore-forming proteins has focused on the structural analysis of monomers and pore-forming oligomeric complexes. We set the family of proteins in context and highlight aspects of their function which the direct and exclusive equation of oligomers with pores fails to explain. Starting with a description of the distribution of MACPF/ CDC proteins across the domains of life, we proceed to show how their evolutionary relationships can be understood on the basis of their structural homology and re-evaluate models for pore formation by perforin, in
particular. We furthermore highlight data showing the role of incomplete oligomeric rings (arcs) in pore formation and how this can explain small pores generated by oligomers of proteins belonging to the family. We set this in the context of cell biological and biophysical data on the proteins’ function and discuss how this helps in the development of an understanding of how they act in processes such as apicomplexan parasites gliding through cells and exiting from cells.
Electronic supplementary material The online version of this article (doi:10.1007/s00018-012-1153-8) contains supplementary material, which is available to authorized users.
Abbreviations ALY Anthrolysin Bth Bacillus thetaiotaomicron MACPF protein CDCs Cholesterol-dependent cytolysins CTL Cytotoxic T lymphocytes EM Electron microscopy GrB Granzyme B ILY Intermedilysin LLO Listeriolysin MACPF Membrane attack complex/perforin MAC Membrane attack complex PFN Perforin PFO Perfringolysin PLY Pneumolysin PLPs Perforin-like proteins Plu Photorhabdus luminescens MACPF protein PPLPs Plasmodium perforin-like proteins PV Parasitophorous vacuole SLO Streptolysin TMH Trans-membrane hairpin (present in the soluble forms of CDC/MACPFs as a-helices)
R. J. C. Gilbert (&) Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK e-mail: [email protected] M. Mikelj G. Anderluh Department of Biology, Biotechnical Faculty, University of Ljubljana, Vecˇna pot 111, 1000 Ljubljana, Slovenia M. Dalla Serra National Research Council, Institute of Biophysics and Bruno Kessler Foundation, via alla Cascata 56/C, 38123 Trento, Italy C. J. Froelich Department of Medicine, NorthShore University HealthSystem Research Institute, Evanston, IL 60201, USA G. Anderluh (&) National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia e-mail: [email protected]
Keywords MACPF domain Cholesterol-dependent cytolysins Pore Membrane interactions Membrane damage
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Introduction This review will discuss lipid membrane interactions by an im
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