TY - GEN A1 - Commichau, Fabian M. T1 - Hochvirulente Isolate des pathogenen Bakteriums Listeria monocytogenes T2 - BioSpektrum N2 - Das Gram-positive Bakterium Listeria monocytogenes kommt sowohl freilebend als auch als Pathogen in verschiedenen Wirbeltiertaxa sowie in Crustaceen vor. Gelangt L. monocytogenes über die Nah- rung in den menschlichen Körper, kann es Listeriose auslösen. Diese bakterielle Infektion ist für immunsupprimierte und ältere Menschen sowie für schwangere Frauen besonders gefährlich. Aufgrund unzureichender hygienischer Maßnahmen bei der Lebensmittelzubereitung kam es in der Vergangenheit immer wieder zu Todesfällen. Kürzlich berichteten Yuelan Yin et al. (Nat Commun (2019) 10:4283) von den virulentesten L. monocytogenes- Isolaten. Y1 - 2020 UR - https://link.springer.com/article/10.1007/s12268-020-1383-5 U6 - https://doi.org/10.1007/s12268-020-1383-5 SN - 1868-6249 SN - 0947-0867 VL - 26 IS - 3 SP - S. 280 ER - TY - GEN A1 - Richts, Björn A1 - Hertel, Robert A1 - Potot, Sébastien A1 - Poehlein, Anja A1 - Daniel, Rolf A1 - Schyns, Ghislain A1 - Prágai, Zoltán A1 - Commichau, Fabian M. T1 - Complete Genome Sequence of the Prototrophic Bacillus subtilis subsp. subtilis Strain SP1 T2 - Microbiology Resource Announcements N2 - Here, we present the complete genome sequence of the Bacillus subtilis strain SP1. This strain is a descendant of the laboratory strain 168. The strain is suit- able for biotechnological applications because the prototrophy for tryptophan has been restored. Due to laboratory cultivation, the strain has acquired 24 additional sequence variations. Y1 - 2020 UR - https://mra.asm.org/content/9/32/e00825-20 U6 - https://doi.org/10.1128/MRA.00825-20 SN - 2576-098X VL - 9 IS - 32 ER - TY - GEN A1 - Lilge, Lars A1 - Hertel, Robert A1 - Morabbi Heravi, Kambiz A1 - Henkel, Marius A1 - Commichau, Fabian M. A1 - Hausmann, Rudolf T1 - Draft Genome Sequence of the Type Strain Bacillus subtilis subsp. subtilis DSM10 T2 - Microbiology Resource Announcements N2 - The Bacillus subtilis subsp. subtilis type strain DSM10 has been used as a reference in various studies. However, detailed information about the genome has not been available. Therefore, whole-genome sequencing was performed, and the sequence was compared with that of the related B. subtilis strain NCIB3610. Y1 - 2021 UR - https://mra.asm.org/content/10/10/e00158-21 U6 - https://doi.org/10.1128/MRA.00158-21 SN - 2576-098X VL - 10 IS - 10 SP - 1 EP - 3 ER - TY - GEN A1 - Commichau, Fabian M. A1 - Lassak, Jürgen T1 - Symposium der VAAM-Fachgruppe Regulation und Signaltransduktion in Prokaryoten: Moonlighting-Proteine und promiskuitive Enzyme T2 - BioSpektrum Y1 - 2020 UR - https://www.biospektrum.de/blatt/d_bs_pdf&_id=1779732 SN - 1868-6249 VL - 26 IS - 6 SP - 661 EP - 662 PB - Springer CY - Heidelberg ER - TY - GEN A1 - Riedel, Ramona A1 - Commichau, Fabian M. A1 - Benndorf, Dirk A1 - Hertel, Robert A1 - Holzer, Katharina A1 - Mardoukhi, Mohammad Saba Yousef A1 - Noack, Laura A1 - Martienssen, Marion T1 - Biodegradation of selected aminophosphonates by the bacterial isolate Ochrobactrum sp. BTU1 T2 - Microbial Research N2 - Aminophosphonates, like glyphosate (GS) or metal chelators such as ethylenediaminetetra(methylenephosphonic acid) (EDTMP), are released on a large scale worldwide. Here, we have characterized a bacterial strain capable of degrading synthetic aminophosphonates. The strain was isolated from LC/MS standard solution. Genome sequencing indicated that the strain belongs to the genus Ochrobactrum. Whole-genome classification using pyANI software to compute a pairwise ANI and other metrics between Brucella assemblies and Ochrobactrum contigs revealed that the bacterial strain is designated as Ochrobactrum sp. BTU1. Degradation batch tests with Ochrobactrum sp. BTU1 and the selected aminophosphonates GS, EDTMP, aminomethylphosphonic acid (AMPA), iminodi(methylene-phosphonic) (IDMP) and ethylaminobis(methylenephosphonic) acid (EABMP) showed that the strain can use all phosphonates as sole phosphorus source during phosphorus starvation. The highest growth rate was achieved with AMPA, while EDTMP and GS were least supportive for growth. Proteome analysis revealed that GS degradation is promoted by C-P lyase via the sarcosine pathway, i.e., initial cleavage at the C-P bond. We also identified C-P lyase to be responsible for degradation of EDTMP, EABMP, IDMP and AMPA. However, the identification of the metabolite ethylenediaminetri(methylenephosphonic acid) via LC/MS analysis in the test medium during EDTMP degradation indicates a different initial cleavage step as compared to GS. For EDTMP, it is evident that the initial cleavage occurs at the C-N bond. The detection of different key enzymes at regulated levels, form the bacterial proteoms during EDTMP exposure, further supports this finding. Y1 - 2024 U6 - https://doi.org/10.1016/j.micres.2024.127600 SN - 0944-5013 VL - 280 SP - 1 EP - 12 ER - TY - GEN A1 - Hertel, Robert A1 - Schöne, Kerstin A1 - Mittelstädt, Carolin A1 - Meißner, Janek A1 - Zschoche, Nick A1 - Collignon, Madeline A1 - Kohler, Christian A1 - Friedrich, Ines A1 - Schneider, Dominik A1 - Hoppert, Michael A1 - Kuhn, Ramona A1 - Schwedt, Inge A1 - Scholz, Patricia A1 - Poehlein, Anja A1 - Martienssen, Marion A1 - Ischebeck, Till A1 - Daniel, Rolf A1 - Commichau, Fabian M. T1 - Characterization of glyphosate-resistant Burkholderia anthina and Burkholderia cenocepacia isolates from a commercial Roundup® solution T2 - Environmental Microbiology Reports N2 - Roundup® is the brand name for herbicide solutions containing glyphosate, which specifically inhibits the 5-enolpyruvyl-shikimate-3-phosphate (EPSP) synthase of the shikimate pathway. The inhibition of the EPSP synthase causes plant death because EPSP is required for biosynthesis of aromatic amino acids. Glyphosate also inhibits the growth of archaea, bacteria, Apicomplexa, algae and fungi possessing an EPSP synthase. Here, we have characterized two glyphosate-resistant bacteria from a Roundup solution. Taxonomic classification revealed that the isolates 1CH1 and 2CH1 are Burkholderia anthina and Burkholderia cenocepacia strains respectively. Both isolates cannot utilize glyphosate as a source of phosphorus and synthesize glyphosate-sensitive EPSP synthase variants. Burkholderia. anthina 1CH1 and B. cenocepacia 2CH1 tolerate high levels of glyphosate because the herbicide is not taken up by the bacteria. Previously, it has been observed that the exposure of soil bacteria to herbicides like glyphosate promotes the development of antibiotic resistances. Antibiotic sensitivity testing revealed that the only the B. cenocepacia 2CH1 isolate showed increased resistance to a variety of antibiotics. Thus, the adaptation of B. anthina 1CH1 and B. cenocepacia 2CH1 to glyphosate did not generally increase the antibiotic resistance of both bacteria. However, our study confirms the genomic adaptability of bacteria belonging to the genus Burkholderia. Y1 - 2022 U6 - https://doi.org/10.1111/1758-2229.13022 SN - 1758-2229 VL - 14 IS - 1 SP - 70 EP - 84 ER - TY - GEN A1 - Wang, Mengyi A1 - Wamp, Sabrina A1 - Gibhardt, Johannes A1 - Holland, Gudrun A1 - Schwedt, Inge A1 - Schmidtke, Kai-Uwe A1 - Scheibner, Katrin A1 - Halbedel, Sven A1 - Commichau, Fabian M. T1 - Adaptation of Listeria monocytogenes to perturbation of c-di-AMP metabolism underpins its role in osmoadaptation and identifies a fosfomycin uptake system T2 - Environmental microbiology N2 - The human pathogen Listeria monocytogenes synthesizes and degrades c-di-AMP using the diadenylate cyclase CdaA and the phosphodiesterases PdeA and PgpH respectively. c-di-AMP is essential because it prevents the uncontrolled uptake of osmolytes. Here, we studied the phenotypes of cdaA, pdeA, pgpH and pdeA pgpH mutants with defects in c-di-AMP metabolism and characterized suppressor mutants restoring their growth defects. The characterization of the pdeA pgpH mutant revealed that the bacteria show growth defects in defined medium, a phenotype that is invariably suppressed by mutations in cdaA. The previously reported growth defect of the cdaA mutant in rich medium is suppressed by mutations that osmotically stabilize the c-di-AMP-free strain. We also found that the cdaA mutant has an increased sensitivity against isoleucine. The isoleucine-dependent growth inhibition of the cdaA mutant is suppressed by codY mutations that likely reduce the DNA-binding activity of encoded CodY variants. Moreover, the characterization of the cdaA suppressor mutants revealed that the Opp oligopeptide transport system is involved in the uptake of the antibiotic fosfomycin. In conclusion, the suppressor analysis corroborates a key function of c-di-AMP in controlling osmolyte homeostasis in L. monocytogenes. KW - Listeria monocytogenes KW - c-di-AMP metabolism Y1 - 2022 UR - https://sfamjournals.onlinelibrary.wiley.com/doi/10.1111/1462-2920.16084?af=R U6 - https://doi.org/10.1111/1462-2920.16084 SN - 1462-2920 VL - 24 IS - 9 SP - 4466 EP - 4488 ER - TY - GEN A1 - Commichau, Fabian M. A1 - Gibhardt, Johannes A1 - Heidemann, Jana A1 - Bremenkamp, Rica A1 - Rosenberg, Jonathan A1 - Seifert, Roland A1 - Kaever, Volkhard A1 - Ficner, Ralf T1 - An extracytoplasmic protein and a moonlighting enzyme modulate synthesis of c-di-AMP in Listeria monocytogenes T2 - Environmental Microbiology N2 - The second messenger cyclic di-AMP (c-di-AMP) is essential for growth of many bacteria because it controls osmolyte homeostasis. c-di-AMP can regulate the synthesis of potassium uptake systems in some bacteria and it also directly inhibits and activates potassium import and export systems, respectively. Therefore, c-di-AMP production and degradation have to be tightly regulated depending on the environmental osmolarity. The Gram-positive pathogen Listeria monocytogenes relies on the membrane-bound diadenylate cyclase CdaA for c-di-AMP production and degrades the nucleotide with two phosphodiesterases. While the enzymes producing and degrading the dinucleotide have been reasonably well examined, the regulation of c-di-AMP production is not well understood yet. Here we demonstrate that the extracytoplasmic regulator CdaR interacts with CdaA via its transmembrane helix to modulate c-di-AMP production. Moreover, we show that the phosphoglucosamine mutase GlmM forms a complex with CdaA and inhibits the diadenylate cyclase activity in vitro. We also found that GlmM inhibits c-di-AMP production in L. monocytogenes when the bacteria encounter osmotic stress. Thus, GlmM is the major factor controlling the activity of CdaA in vivo. GlmM can be assigned to the class of moonlighting proteins because it is active in metabolism and adjusts the cellular turgor depending on environmental osmolarity. Y1 - 2020 UR - https://sfamjournals.onlinelibrary.wiley.com/doi/full/10.1111/1462-2920.15008 U6 - https://doi.org/10.1111/1462-2920.15008 SN - 1462-2920 SN - 1462-2912 VL - 22 IS - 7 SP - 2771 EP - 2791 ER - TY - GEN A1 - Hertel, Robert A1 - Gibhardt, Johannes A1 - Martienssen, Marion A1 - Kuhn, Ramona A1 - Commichau, Fabian M. T1 - Molecular mechanisms underlying glyphosate resistance in bacteria T2 - Environmental Microbiology N2 - Glyphosate is a nonselective herbicide that kills weeds and other plants competing with crops. Glyphosate specifically inhibits the 5-enolpyruvyl-shikimate-3-phosphate (EPSP) synthase, thereby depleting the cell of EPSP serving as a precursor for biosynthesis of aromatic amino acids. Glyphosate is considered to be toxicologically safe for animals and humans. Therefore, it became the most-important herbicide in agriculture. However, its intensive application in agriculture is a serious environmental issue because it may negatively affect the biodiversity. A few years after the discovery of the mode of action of glyphosate, it has been observed that bacteria evolve glyphosate resistance by acquiring mutations in the EPSP synthase gene, rendering the encoded enzyme less sensitive to the herbicide. The identification of glyphosate-resistant EPSP synthase variants paved the way for engineering crops tolerating increased amounts of the herbicide. This review intends to summarize the molecular mechanisms underlying glyphosate resistance in bacteria. Bacteria can evolve glyphosate resistance by (i) reducing glyphosate sensitivity or elevating production of the EPSP synthase, by (ii) degrading or (iii) detoxifying glyphosate and by (iv) decreasing the uptake or increasing the export of the herbicide. The variety of glyphosate resistance mechanisms illustrates the adaptability of bacteria to anthropogenic substances due to genomic alterations. Y1 - 2021 U6 - https://doi.org/10.1111/1462-2920.15534 SN - 1462-2920 SN - 1462-2912 VL - 23 IS - 6 SP - 2891 EP - 2905 ER - TY - GEN A1 - Schwedt, Inge A1 - Schöne, Kerstin A1 - Eckert, Maike A1 - Pizzinato, Manon A1 - Winkler, Laura A1 - Knotkova, Barbora A1 - Richts, Björn A1 - Hau, Jann‐Louis A1 - Steuber, Julia A1 - Mireles, Raul A1 - Noda‐Garcia, Lianet A1 - Fritz, Günter A1 - Mittelstädt, Carolin A1 - Hertel, Robert A1 - Commichau, Fabian M. T1 - The low mutational flexibility of the EPSP synthase in Bacillus subtilis is due to a higher demand for shikimate pathway intermediates T2 - Environmental Microbiology N2 - Glyphosate (GS) inhibits the 5-enolpyruvyl-shikimate-3-phosphate (EPSP) synthase that is required for aromatic amino acid, folate and quinone biosynthesis in Bacillus subtilis and Escherichia coli. The inhibition of the EPSP synthase by GS depletes the cell of these metabolites, resulting in cell death. Here, we show that like the laboratory B. subtilis strains also environmental and undomesticated isolates adapt to GS by reducing herbicide uptake. Although B. subtilis possesses a GS-insensitive EPSP synthase, the enzyme is strongly inhibited by GS in the native environment. Moreover, the B. subtilis EPSP synthase mutant was only viable in rich medium containing menaquinone, indicating that the bacteria require a catalytically efficient EPSP synthase under nutrient-poor conditions. The dependency of B. subtilis on the EPSP synthase probably limits its evolvability. In contrast, E. coli rapidly acquires GS resistance by target modification. However, the evolution of a GS-resistant EPSP synthase under non-selective growth conditions indicates that GS resistance causes fitness costs. Therefore, in both model organisms, the proper function of the EPSP synthase is critical for the cellular viability. This study also revealed that the uptake systems for folate precursors, phenylalanine and tyrosine need to be identified and characterized in B. subtilis. Y1 - 2023 U6 - https://doi.org/10.1111/1462-2920.16518 SN - 1462-2912 SN - 1462-2920 VL - 25 IS - 12 SP - 3604 EP - 3622 ER -