Structure and assembly of the S-layer in C. difficile

Abstract

Many bacteria and archaea possess a two-dimensional protein array, or S-layer, that covers the cell surface and plays crucial roles in cell physiology. Here, we report the crystal structure of SlpA, the main S-layer protein of the bacterial pathogen Clostridioides difficile, and use electron microscopy to study S-layer organisation and assembly. The SlpA crystal lattice mimics S-layer assembly in the cell, through tiling of triangular prisms above the cell wall, interlocked by distinct ridges facing the environment. Strikingly, the array is very compact, with pores of only ~10 Å in diameter, compared to other S-layers (30–100 Å). The surface-exposed flexible ridges are partially dispensable for overall structure and assembly, although a mutant lacking this region becomes susceptible to lysozyme, an important molecule in host defence. Thus, our work gives insights into S-layer organisation and provides a basis for development of C. difficile-specific therapeutics.

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Item Type:	Article
Authors/Creators:	Lanzoni-Mangutchi, P. Banerji, O. Wilson, J. https://orcid.org/0000-0002-6967-0809 Barwinska-Sendra, A. Kirk, J.A. Vaz, F. O’Beirne, S. Baslé, A. El Omari, K. Wagner, A. Fairweather, N.F. Douce, G.R. Bullough, P.A. https://orcid.org/0000-0001-8147-1127 Fagan, R.P. https://orcid.org/0000-0002-8704-4828 Salgado, P.S.
Copyright, Publisher and Additional Information:	© 2022 The Author(s). This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
Dates:	Published: 25 February 2022 Published (online): 25 February 2022 Accepted: 6 January 2022
Institution:	The University of Sheffield
Academic Units:	The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield)
Funding Information:	Funder Grant number Biotechnology and Biological Sciences Research Council BB/P02002X/1 The Wellcome Trust 204877/Z/16/Z
Depositing User:	Symplectic Sheffield
Date Deposited:	28 Feb 2022 11:12
Last Modified:	10 Feb 2023 14:12
Status:	Published
Publisher:	Springer Nature
Refereed:	Yes
Identification Number:	10.1038/s41467-022-28196-w
Open Archives Initiative ID (OAI ID):	oai:eprints.whiterose.ac.uk:184166

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Structure and assembly of the S-layer in C. difficile

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