Evidence for an adaptation of a phage-derived holin/endolysin system to toxin transport in Clostridioides difficile

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dc.identifier.uri http://dx.doi.org/10.15488/4242
dc.identifier.uri https://www.repo.uni-hannover.de/handle/123456789/4276
dc.contributor.author Mehner-Breitfeld, Denise
dc.contributor.author Rathmann, Claudia
dc.contributor.author Riedel, Thomas
dc.contributor.author Just, Ingo
dc.contributor.author Gerhard, Ralf
dc.contributor.author Overmann, Jörg
dc.contributor.author Brüser, Thomas
dc.date.accessioned 2018-12-20T14:20:22Z
dc.date.available 2018-12-20T14:20:22Z
dc.date.issued 2018
dc.identifier.citation Mehner-Breitfeld, D.; Rathmann, C.; Riedel, T.; Just, I.; Gerhard, R. et al.: Evidence for an adaptation of a phage-derived holin/endolysin system to toxin transport in Clostridioides difficile. In: Frontiers in Microbiology 9 (2018), 2446. DOI: https://doi.org/10.3389/fmicb.2018.02446
dc.description.abstract The pathogenicity locus (PaLoc) of Clostridioides difficile usually comprises five genes (tcdR, tcdB, tcdE, tcdA, tcdC). While the proteins TcdA and TcdB represent the main toxins of this pathogen, TcdR and TcdC are involved in the regulation of their production. TcdE is a holin family protein, members of which are usually involved in the transport of cell wall-degrading enzymes (endolysins) for phage-induced lysis. In the past, TcdE has been shown to contribute to the release of TcdA and TcdB, but it is unclear whether it mediates a specific transport or rather a lysis of cells. TcdE of C. difficile strains analyzed so far can be produced in three isoforms that are initiated from distinct N-terminal ATG codons. When produced in Escherichia coli, we found that the longest TcdE isoform had a moderate effect on cell growth, whereas the shortest isoform strongly induced lysis. The effect of the longest isoform was inhibitory for cell lysis, implying a regulatory function of the N-terminal 24 residues. We analyzed the PaLoc sequence of 44 C. difficile isolates and found that four of these apparently encode only the short TcdE isoforms, and the most closely related holins from C. difficile phages only possess one of these initiation codons, indicating that an N-terminal extension of TcdE evolved in C. difficile. All PaLoc sequences comprised also a conserved gene encoding a short fragment of an endolysin remnant of a phage holin/endolysin pair. We could produce this peptide, which we named TcdL, and demonstrated by bacterial two-hybrid analysis a self-interaction and an interaction with TcdB that might serve to mediate TcdE-dependent transport. eng
dc.language.iso eng
dc.publisher Lausanne : Frontiers Media S.A.
dc.relation.ispartofseries Frontiers in Microbiology 9 (2018)
dc.rights CC BY 4.0 Unported
dc.rights.uri https://creativecommons.org/licenses/by/4.0/
dc.subject Clostridioides difficile eng
dc.subject Endolysins eng
dc.subject Holins eng
dc.subject Protein transport eng
dc.subject Toxins eng
dc.subject.ddc 570 | Biowissenschaften, Biologie ger
dc.title Evidence for an adaptation of a phage-derived holin/endolysin system to toxin transport in Clostridioides difficile
dc.type article
dc.type Text
dc.relation.issn 1664302X
dc.relation.doi https://doi.org/10.3389/fmicb.2018.02446
dc.bibliographicCitation.volume 9
dc.bibliographicCitation.firstPage 2446
dc.description.version publishedVersion
tib.accessRights frei zug�nglich

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