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

Paola Lanzoni-Mangutchi, Oishik Banerji, Jason Wilson, Anna Barwinska-Sendra, Joseph A. Kirk, Filipa Vaz, Shauna O’Beirne, Arnaud Baslé, Kamel El Omari, Armin Wagner, Neil F. Fairweather, Gillian R. Douce, Per A. Bullough (), Robert P. Fagan () and Paula S. Salgado ()
Additional contact information
Paola Lanzoni-Mangutchi: Newcastle University
Oishik Banerji: University of Sheffield
Jason Wilson: University of Sheffield
Anna Barwinska-Sendra: Newcastle University
Joseph A. Kirk: University of Sheffield
Filipa Vaz: University of Glasgow
Shauna O’Beirne: University of Sheffield
Arnaud Baslé: Newcastle University
Kamel El Omari: Diamond Light Source
Armin Wagner: Diamond Light Source
Neil F. Fairweather: Imperial College London
Gillian R. Douce: University of Glasgow
Per A. Bullough: University of Sheffield
Robert P. Fagan: University of Sheffield
Paula S. Salgado: Newcastle University

Nature Communications, 2022, vol. 13, issue 1, 1-13

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41467-022-28196-w

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