8opr: Difference between revisions
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/SLAP2_BACAN SLAP2_BACAN] The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of bacteria. | [https://www.uniprot.org/uniprot/SLAP2_BACAN SLAP2_BACAN] The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of bacteria. | ||
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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<ref>PMID:37923757</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
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</StructureSection> | </StructureSection> | ||
Latest revision as of 14:45, 6 November 2024
Structure of the EA1 surface layer of Bacillus anthracis
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