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The structure of Macrophage Expressed Gene-1, a phagolysosome immune effector that is activated upon acidification.

S. S. Pang, C. Bayly-Jones, M. Radjainia, B. A. Spicer, R. H. P. Law, A. W. Hodel, S. M. Ekkel, P. J. Conroy, G. Ramm, H. Venugopal, P. I. Bird, B. W. Hoogenboom, I. Voskoboinik, Y. Gambin, E. Sierecki, M. A. Dunstone, J. C. Whisstock

Abstract

Macrophage Expressed Gene-1 (MPEG-1; also termed Perforin-2) is an endosomal / phagolysosomal perforin-like protein that is conserved across the metazoan kingdom and that functions within the phagolysosome to damage engulfed microbes. Like the Membrane Attack Complex and perforin, MPEG-1 has been postulated to form pores in target membranes, however, its mode of action remains to be established. We used single particle cryo-Electron Microscopy to determine the 2.4 [A] structure of a hexadecameric assembly of MPEG-1 that displays the expected features of a soluble pre-pore complex. We further discovered that the MPEG-1 pre-pore-like assemblies can be induced to perforate membranes through mild acidification, such as would occur within maturing phagolysosomes. We next solved the 3.6 [A] cryo-EM structure of MPEG-1 in complex with liposomes. Remarkably these data revealed that a C-terminal Multi-vesicular body of 12 kDa (MVB12)-associated {beta}-prism (MABP) domain interacts with target membranes in a mode that positions the pore forming machinery of MPEG-1 to point away from the bound membrane. This unexpected mechanism of membrane interaction raises the intriguing possibility that MPEG-1 may be able to remain bound to the phagolysosome membrane while simultaneously forming pores in engulfed bacterial targets.

PDFDOI

02 /Specification & Classification

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