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

Lookup NU author(s): Paola Lanzoni, Dr Anna Barwinska-SendraORCiD, Dr Arnaud Basle, Professor Paula SalgadoORCiD

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This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).

Abstract

© 2022, The Author(s).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.

Publication metadata

Author(s): Lanzoni-Mangutchi P, Banerji O, Wilson J, Barwinska-Sendra A, Kirk JA, Vaz F, O'Beirne S, Basle A, El Omari K, Wagner A, Fairweather NF, Douce GR, Bullough PA, Fagan RP, Salgado PS

Publication type: Article

Publication status: Published

Journal: Nature Communications

Year: 2022

Volume: 13

Issue: 1

Print publication date: 01/12/2022

Online publication date: 25/02/2022

Acceptance date: 06/01/2022

Date deposited: 14/03/2022

ISSN (electronic): 2041-1723

Publisher: Nature Research

URL: https://doi.org/10.1038/s41467-022-28196-w

DOI: 10.1038/s41467-022-28196-w

PubMed id: 35217634

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