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Beyond difficile: three novel toxin B-producing Clostridioides species from human patients with diarrhea (spore proteome)

ABSTRACT: Clostridioides difficile infection (CDI), caused by strains producing toxin B (TcdB), poses a significant global health threat. While C. difficile exhibits substantial diversity, functional studies have focused on a limited number of isolates, overlooking other genomospecies within the genus. We describe five isolates from patients suspected of having CDI who tested negative for the PaLoc marker gene tcdC. Through genomic, proteomic, and phenotypic analyses, we demonstrate that they correspond to three novel toxin-producing species, designated as Clostridioides cryptodifficilis sp. nov., Clostridioides divergens sp. nov., and Clostridioides subdifficilis sp. nov. These species are distinguished by unique MALDI-ToF signatures, metabolic capabilities, and genomic and proteomic architectures, underscoring their clear taxonomic and functional divergence from C. difficile. They secrete functionally active TcdB7 or TcdB11, as demonstrated by cytotoxicity assays in cultured cells and in vivo using the mouse ileal loop model, implicating them in disease pathology, albeit with lower virulence than C. difficile. Our findings expand the known diversity of TcdB-producing Clostridioides and have direct implications for diagnostics, surveillance, and clinical management of diarrheal diseases.

INSTRUMENT(S):

ORGANISM(S): Clostridioides Sp.

SUBMITTER: Anke Trautwein-Schult

LAB HEAD: Prof. Dr. Dörte becher

PROVIDER: PXD066931 | Pride | 2026-05-06

REPOSITORIES: Pride

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			Action	DRS
	20230126_DSM_113156_113158_113160_113161_113162_113163_29319_28645_27147_102978_28669_29747_nr_95.fasta	Fasta
	230227_OV3_P3_JB_ATS_2022_039_CDbiOmicsSpores_180min_2809_A.raw	Raw
	230227_OV3_P3_JB_ATS_2022_039_CDbiOmicsSpores_180min_7678_A.raw	Raw
	230227_OV3_P3_JB_ATS_2022_039_CDbiOmicsSpores_180min_8947_A.raw	Raw
	230227_OV3_P3_JB_ATS_2022_039_CDbiOmicsSpores_180min_8949_A.raw	Raw

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Project description:Bacterial spores play an important role in disease initiation, transmission and persistence. The outermost spore layer, the exosporium, is important as it is the first point of contact between the spore and the environment and may be involved in spore adherence, protection and germination. Clostridium sordellii is a highly lethal, spore forming pathogen that causes soft-tissue infections, enteritis and toxic-shock syndrome. Despite the importance of C. sordellii spores in disease, spore proteins from this bacterium have not been defined or interrogated functionally. In this study, we identified the C. sordellii outer spore proteome and two of the identified proteins, CSA and CSB, were characterised using a genetic and phenotypic approach. Both proteins were essential for the correct formation and positioning of the C. sordellii spore coat and exosporium. The absence of CSA reduced sporulation levels and increased spore sensitivity to heat, sodium hydroxide and hydrochloric acid. By comparison, CSB was required for normal levels of spore adherence to cervical, but not vaginal, cells, with csb mutant spores having increased adherence properties. The establishment of a mouse infection model of the gastrointestinal tract for C. sordellii allowed the role of CSA and CSB to be interrogated in an infected host. Following the oral administration of spores to mice, the wild-type strain efficiently colonized the gastrointestinal tract, with the peak of bacterial numbers occurring at one day post-infection. Colonization was reduced by two logs at four days post-infection. By comparison, mice infected with the csb mutant did not show a reduction in bacterial numbers. The absence of CSB therefore allows the csb mutant to persist within the gastrointestinal tract. We conclude that C. sordellii outer spore proteins are important for the structural and functional integrity of spores, and for colonization and persistence during infection. Finally, Clostridium difficile, Bacillus cereus and Bacillus anthracis encode proteins with homology to CSA and CSB but these bacteria produce spores that are structurally dissimilar to those of C. sordellii, and the function of the proteins in these hosts is different to that in C. sordellii. These findings suggest that, despite their homology, spore proteins can have variable functions in different bacterial species which highlights the necessity of studying each spore protein in the cognate species from which it originates.

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Beyond difficile: three novel toxin B-producing Clostridioides species from human patients with diarrhea (spore proteome)

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