Abstract
Proteins with membrane-attack complex/perforin (MACPF) domains are found in almost all kingdoms of life, and they have a variety of biological roles, including defence and attack, organism development, and cell adhesion and signalling. The distribution of these proteins in fungi appears to be restricted to some Pezizomycotina and Basidiomycota species only, in correlation with another group of proteins with unknown biological function, known as aegerolysins. These two protein groups coincide in only a few species, and they might operate in concert as cytolytic bi-component pore-forming agents. Representative proteins here include pleurotolysin B, which has a MACPF domain, and the aegerolysin-like protein pleurotolysin A, and the very similar ostreolysin A, which have been purified from oyster mushroom (Pleurotus ostreatus). These have been shown to act in concert to perforate natural and artificial lipid membranes with high cholesterol and sphingomyelin content. The aegerolysin-like proteins provide the membrane cholesterol/sphingomyelin selectivity and recruit oligomerised pleurotolysin B molecules, to create a membrane-inserted pore complex. The resulting protein structure has been imaged with electron microscopy, and it has a 13-meric rosette-like structure, with a central lumen that is ~4–5 nm in diameter. The opened transmembrane pore is non-selectively permeable for ions and smaller neutral solutes, and is a cause of cytolysis of a colloid-osmotic type. The biological significance of these proteins for the fungal life-style is discussed.
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Abbreviations
- 3D:
-
Three-dimensional
- diΦPC:
-
diphytanoylphosphatidylcholine
- EGFP:
-
Enhanced green fluorescent protein
- Hi:
-
H. irregulare
- LUV:
-
Large unilamellar vesicles
- MACPF:
-
Membrane-attack complex/perforin
- Mp:
-
M. perniciosa
- OlyA:
-
Ostreolysin A
- PLM:
-
Planar lipid membranes
- PlyA:
-
Pleurotolysin A
- PlyA2:
-
Pleurotolysin A2
- PlyB:
-
Pleurotolysin B
- Ss:
-
S. stellatus
- Tv:
-
T. versicolor
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Acknowledgments
GV and MDS thank the Laboratory of Biomolecular Sequence and Structure Analysis for Health (LaBSSAH) for technical support. The Slovenian authors were supported by the Slovenian Research Agency (contracts P1-0207 and J1-4305). The authors thank Christopher Berrie for editorial revision of the manuscript.
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Ota, K., Butala, M., Viero, G., Dalla Serra, M., Sepčić, K., Maček, P. (2014). Fungal MACPF-Like Proteins and Aegerolysins: Bi-component Pore-Forming Proteins?. In: Anderluh, G., Gilbert, R. (eds) MACPF/CDC Proteins - Agents of Defence, Attack and Invasion. Subcellular Biochemistry, vol 80. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-8881-6_14
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