ArticleMolecular microbiology2018
Differential requirements for conserved peptidoglycan remodeling enzymes during Clostridioides difficile spore formation.
Article in Molecular microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 29 citations in OpenAlex.
- Penicillin-binding proteins exhibit functional redundancy during asymmetric cell division inJournal of bacteriology · 2025Article
- The small acid-soluble proteins of Clostridioides difficile regulate sporulation in a SpoIVB2-dependent manner.PLoS pathogens · 2024Article
- Cleavage of an engulfment peptidoglycan hydrolase by a sporulation signature protease in Clostridioides difficile.Molecular microbiology · 2024Article
- The small acid-soluble proteins ofbioRxiv : the preprint server for biology · 2024Article
- Clostridioides difficile Sporulation.Advances in experimental medicine and biology · 2024Review
- Conservation and Evolution of the Sporulation Gene Set in Diverse Members of theJournal of bacteriology · 2022Article
- Article
- Distribution and preservation of the components of the engulfment. What is beyond representative genomes?PloS one · 2021Article
- Structural, Metabolic and Evolutionary Comparison of Bacterial Endospore and Exospore Formation.Frontiers in microbiology · 2021Review
- Milestones inMicrobial cell (Graz, Austria) · 2020Review
- Role of SpoIVA ATPase Motifs during Clostridioides difficile Sporulation.Journal of bacteriology · 2020Article
- Development of Strong Anaerobic Fluorescent Reporters for Clostridium acetobutylicum and Clostridium ljungdahlii Using HaloTag and SNAP-tag Proteins.Applied and environmental microbiology · 2020Article
- Shaping an Endospore: Architectural Transformations DuringAnnual review of microbiology · 2020Review
- Epigenomic characterization of Clostridioides difficile finds a conserved DNA methyltransferase that mediates sporulation and pathogenesis.Nature microbiology · 2020Article
- From Root to Tips: Sporulation Evolution and Specialization in Bacillus subtilis and the Intestinal Pathogen Clostridioides difficile.Molecular biology and evolution · 2019Article
- Article
- Clostridial Genetics: Genetic Manipulation of the Pathogenic Clostridia.Microbiology spectrum · 2019Review
- SpoIVA-SipL Complex Formation Is Essential forJournal of bacteriology · 2019Article
- Peptidoglycan degradation machinery in Clostridium difficile forespore engulfment.Molecular microbiology · 2018Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Spore formation is essential for the bacterial pathogen and obligate anaerobe, Clostridioides (Clostridium) difficile, to transmit disease. Completion of this process depends on the mother cell engulfing the developing forespore, but little is known about how engulfment occurs in C. difficile. In Bacillus subtilis, engulfment is mediated by a peptidoglycan degradation complex consisting of SpoIID, SpoIIP and SpoIIM, which are all individually required for spore formation. Using genetic analyses, we determined the functions of these engulfment-related proteins along with the putative endopeptidase, SpoIIQ, during C. difficile sporulation. While SpoIID, SpoIIP and SpoIIQ were critical for engulfment, loss of SpoIIM minimally impacted C. difficile spore formation. Interestingly, a small percentage of ∆spoIID and ∆spoIIQ cells generated heat-resistant spores through the actions of SpoIIQ and SpoIID, respectively. Loss of SpoIID and SpoIIQ also led to unique morphological phenotypes: asymmetric engulfment and forespore distortions, respectively. Catalytic mutant complementation analyses revealed that these phenotypes depend on the enzymatic activities of SpoIIP and SpoIID, respectively. Lastly, engulfment mutants mislocalized polymerized coat even though the basement layer coat proteins, SpoIVA and SipL, remained associated with the forespore. Collectively, these findings advance our understanding of several stages during infectious C. difficile spore assembly.
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