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Publication Abstract from PubMed

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.

Structure and function of the EA1 surface layer of Bacillus anthracis.,Sogues A, Fioravanti A, Jonckheere W, Pardon E, Steyaert J, Remaut H Nat Commun. 2023 Nov 3;14(1):7051. doi: 10.1038/s41467-023-42826-x. PMID:37923757^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.