Structural basis for tuning activity and membrane specificity of bacterial cytolysins

Nita R. Shah; Tomas B. Voisin; Edward S. Parsons; Courtney M. Boyd; Bart W. Hoogenboom; Doryen Bubeck

doi:10.1038/s41467-020-19482-6

Nature Communications (Nov 2020)

Structural basis for tuning activity and membrane specificity of bacterial cytolysins

Nita R. Shah,
Tomas B. Voisin,
Edward S. Parsons,
Courtney M. Boyd,
Bart W. Hoogenboom,
Doryen Bubeck

Affiliations

Nita R. Shah: Department of Life Sciences, Sir Ernst Chain Building, Imperial College London
Tomas B. Voisin: Department of Life Sciences, Sir Ernst Chain Building, Imperial College London
Edward S. Parsons: London Centre for Nanotechnology, University College London
Courtney M. Boyd: Department of Life Sciences, Sir Ernst Chain Building, Imperial College London
Bart W. Hoogenboom: London Centre for Nanotechnology, University College London
Doryen Bubeck: Department of Life Sciences, Sir Ernst Chain Building, Imperial College London

DOI: https://doi.org/10.1038/s41467-020-19482-6
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 10

Abstract

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Cholesterol-dependent cytolysins (CDCs) are bacterial pore-forming virulence factors. Cryo-EM structure of an early conformation of the CDC ILY from Streptococcus intermedius, bound to the human immune receptor CD59, provides insight into ILY oligomerization and role of cholesterol in membrane lysis.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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