Structure and function of the EA1 surface layer of Bacillus anthracis

Adrià Sogues (), Antonella Fioravanti, Wim Jonckheere, Els Pardon, Jan Steyaert and Han Remaut ()
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Adrià Sogues: Structural and Molecular Microbiology, VIB-VUB Center for Structural Biology, VIB
Antonella Fioravanti: Structural and Molecular Microbiology, VIB-VUB Center for Structural Biology, VIB
Wim Jonckheere: Structural and Molecular Microbiology, VIB-VUB Center for Structural Biology, VIB
Els Pardon: Structural Biology Brussels, Vrije Universiteit Brussel, VUB
Jan Steyaert: Structural Biology Brussels, Vrije Universiteit Brussel, VUB
Han Remaut: Structural and Molecular Microbiology, VIB-VUB Center for Structural Biology, VIB

Nature Communications, 2023, vol. 14, issue 1, 1-13

Abstract: Abstract The Gram-positive spore-forming bacterium Bacillus anthracis is the causative agent of anthrax, a deadly disease mostly affecting wildlife and livestock, as well as representing a bioterrorism threat. Its cell surface is covered by the mutually exclusive S-layers Sap and EA1, found in early and late growth phases, respectively. Here we report the nanobody-based structural characterization of EA1 and its native lattice contacts. The EA1 assembly domain consists of 6 immunoglobulin-like domains, where three calcium-binding sites structure interdomain contacts that allow monomers to adopt their assembly-competent conformation. Nanobody-induced depolymerization of EA1 S-layers results in surface defects, membrane blebbing and cell lysis under hypotonic conditions, indicating that S-layers provide additional mechanical stability to the cell wall. Taken together, we report a complete model of the EA1 S-layer and present a set of nanobodies that may have therapeutic potential against Bacillus anthracis.

Date: 2023
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DOI: 10.1038/s41467-023-42826-x

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