ArticleThe Journal of biological chemistry2015
Cyclic diGMP regulates production of sortase substrates of Clostridium difficile and their surface exposure through ZmpI protease-mediated cleavage.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 64 citations in OpenAlex.
- Nanoluciferase-Based Reporters for Clostridioides difficile.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Extracellular DNA filaments associated with surface polysaccharide II give Clostridioides difficile biofilm matrix a network-like structure.NPJ biofilms and microbiomes · 2025Article
- The current riboswitch landscape inMicrobiology (Reading, England) · 2024Review
- c-di-AMP signaling is required for bile salt resistance, osmotolerance, and long-term host colonization byScience signaling · 2022Article
- Coordinated modulation of multiple processes through phase variation of a c-di-GMP phosphodiesterase in Clostridioides difficile.PLoS pathogens · 2022Article
- cAMP and c-di-GMP synergistically support biofilm maintenance through the direct interaction of their effectors.Nature communications · 2022Article
- The divergent roles of sortase in the biology of Gram-positive bacteria.Cell surface (Amsterdam, Netherlands) · 2021Review
- Phylogenetic analysis of the bacterial Pro-Pro-endopeptidase domain reveals a diverse family including secreted and membrane anchored proteins.Current research in microbial sciences · 2021Review
- Phase-variable expression of pdcB, a phosphodiesterase, influences sporulation in Clostridioides difficile.Molecular microbiology · 2021Article
- Biofilm regulation in Clostridioides difficile: Novel systems linked to hypervirulence.PLoS pathogens · 2021Review
- An RNA-centric global view ofProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- Extracellular DNA, cell surface proteins and c-di-GMP promote biofilm formation in Clostridioides difficile.Scientific reports · 2021Article
- Type I toxin-antitoxin systems contribute to the maintenance of mobile genetic elements in Clostridioides difficile.Communications biology · 2020Article
- Bacterial second messenger 3',5'-cyclic diguanylate attracts Caenorhabditis elegans and suppresses its immunity.Communications biology · 2020Article
- How the Anaerobic EnteropathogenmBio · 2020Article
- Clostridium difficile clade 3 (RT023) have a modified cell surface and contain a large transposable island with novel cargo.Scientific reports · 2019Article
- Phase variation of a signal transduction system controls Clostridioides difficile colony morphology, motility, and virulence.PLoS biology · 2019Article
- Molecular determinants of the mechanism and substrate specificity ofThe Journal of biological chemistry · 2019Article
- Clostridial Genetics: Genetic Manipulation of the Pathogenic Clostridia.Microbiology spectrum · 2019Review
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
In Gram-positive pathogens, surface proteins may be covalently anchored to the bacterial peptidoglycan by sortase, a cysteine transpeptidase enzyme. In contrast to other Gram-positive bacteria, only one single sortase enzyme, SrtB, is conserved between strains of Clostridium difficile. Sortase-mediated peptidase activity has been reported in vitro, and seven potential substrates have been identified. Here, we demonstrate the functionality of sortase in C. difficile. We identify two sortase-anchored proteins, the putative adhesins CD2831 and CD3246, and determine the cell wall anchor structure of CD2831. The C-terminal PPKTG sorting motif of CD2831 is cleaved between the threonine and glycine residues, and the carboxyl group of threonine is amide-linked to the side chain amino group of diaminopimelic acid within the peptidoglycan peptide stem. We show that CD2831 protein levels are elevated in the presence of high intracellular cyclic diGMP (c-diGMP) concentrations, in agreement with the control of CD2831 expression by a c-diGMP-dependent type II riboswitch. Low c-diGMP levels induce the release of CD2831 and presumably CD3246 from the surface of cells. This regulation is mediated by proteolytic cleavage of CD2831 and CD3246 by the zinc metalloprotease ZmpI, whose expression is controlled by a type I c-diGMP riboswitch. These data reveal a novel regulatory mechanism for expression of two sortase substrates by the secondary messenger c-diGMP, on which surface anchoring is dependent.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.