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A sporulation signature protease is required for assembly of the spore surface layers, germination and host colonization in Clostridioides difficile

2023-11Artigo científico Acesso aberto
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dc.contributor.authorMarini, Eleonora
dc.contributor.authorOlivença, Carmen
dc.contributor.authorRamalhete, Sara
dc.contributor.authorAguirre, Andrea Martinez
dc.contributor.authorIngle, Patrick
dc.contributor.authorMelo, Manuel N.
dc.contributor.authorAntunes, Wilson
dc.contributor.authorMinton, Nigel P.
dc.contributor.authorHernandez, Guillem
dc.contributor.authorCordeiro, Tiago N.
dc.contributor.authorSorg, Joseph A.
dc.contributor.authorSerrano, Mónica
dc.contributor.authorHenriques, Adriano O.
dc.contributor.institutionInstituto de Tecnologia Química e Biológica António Xavier (ITQB)
dc.contributor.pblPLOS - Public Library of Science
dc.date.accessioned2024-04-01T23:57:21Z
dc.date.available2024-04-01T23:57:21Z
dc.date.issued2023-11
dc.descriptionPublisher Copyright: Copyright: © 2023 Marini et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
dc.description.abstractA genomic signature for endosporulation includes a gene coding for a protease, YabG, which in the model organism Bacillus subtilis is involved in assembly of the spore coat. We show that in the human pathogen Clostridioidesm difficile, YabG is critical for the assembly of the coat and exosporium layers of spores. YabG is produced during sporulation under the control of the mother cell-specific regulators σE and σK and associates with the spore surface layers. YabG shows an N-terminal SH3-like domain and a C-terminal domain that resembles single domain response regulators, such as CheY, yet is atypical in that the conserved phosphoryl-acceptor residue is absent. Instead, the CheY-like domain carries residues required for activity, including Cys207 and His161, the homologues of which form a catalytic diad in the B. subtilis protein, and also Asp162. The substitution of any of these residues by Ala, eliminates an auto-proteolytic activity as well as interdomain processing of CspBA, a reaction that releases the CspB protease, required for proper spore germination. An in-frame deletion of yabG or an allele coding for an inactive protein, yabGC207A, both cause misassemby of the coat and exosporium and the formation of spores that are more permeable to lysozyme and impaired in germination and host colonization. Furthermore, we show that YabG is required for the expression of at least two σK-dependent genes, cotA, coding for a coat protein, and cdeM, coding for a key determinant of exosporium assembly. Thus, YabG also impinges upon the genetic program of the mother cell possibly by eliminating a transcriptional repressor. Although this activity has not been described for the B. subtilis protein and most of the YabG substrates vary among sporeformers, the general role of the protease in the assembly of the spore surface is likely to be conserved across evolutionary distance.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent4274720
dc.identifier.doi10.1371/journal.ppat.1011741
dc.identifier.issn1553-7366
dc.identifier.otherPURE: 84639745
dc.identifier.otherPURE UUID: cb2a4b4c-49ca-40ea-aaa1-16be61946bf7
dc.identifier.otherScopus: 85176772102
dc.identifier.otherPubMed: 37956166
dc.identifier.urihttp://hdl.handle.net/10362/165689
dc.identifier.urlhttps://www.scopus.com/pages/publications/85176772102
dc.language.isoeng
dc.peerreviewedyes
dc.subjectParasitology
dc.subjectMicrobiology
dc.subjectImmunology
dc.subjectMolecular Biology
dc.subjectGenetics
dc.subjectVirology
dc.titleA sporulation signature protease is required for assembly of the spore surface layers, germination and host colonization in Clostridioides difficileen
dc.typejournal article
degois.publication.issue11
degois.publication.titlePLoS Pathogens
degois.publication.volume19
dspace.entity.typePublication
rcaap.rightsopenAccess

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