atcc str profile database  (ATCC)

Journal: bioRxiv

Article Title: The cytoplasmic C-terminal domain of the MmpL11 lipid transporter is required for interaction with its co-cistronic partner MSMEG_0240 in Mycobacterium smegmatis

doi: 10.64898/2026.01.19.699910

Figure Lengend Snippet: (A) Schematic representation of the different constructs that were generated in this study. Due to toxicity and/or production issues, only constructs 1, 2, 6, 7 and 8 were further used for BioID analyses. (B) Anti-HA Western blot analysis of total lysates from two independent clones of Msm mc²155 transformed with pMV361_ Nter (truncated), pMV361_ mmpL11 (full-length), pMV361_ Nter-birA or pMV361_ mmpL11-birA , as indicated. (C) OD600nm values at 16 and 40 h from cultures of Msm mc²155 transformed with empty pMV361 (in black), pMV361_ birA (in red), pMV361_ Nter (in green), pMV361_ mmpL11 (in blue), pMV361_ Nter-birA (in orange) or pMV361_ mmpL11-birA (in purple). (D) and (E) Western blot analyses using anti-HA antibodies or HRP-conjugated streptavidin of biotinylated proteins from total lysates of Msm mc²155 transformed with pMV361, pMV361_ birA , pMV361_ Nter , pMV361_ Nter-birA , pMV361_ mmpL11 or pMV361_ mmpL11-birA , after enrichment on streptavidin beads. The molecular size markers (M) with their respective sizes expressed in kDa are shown on the left. The positions of MmpL11-BirA (140 kDa), Nter-BirA (110 kDa) and BirA (37 kDa) are indicated by the short horizontal bars. Images are representative of three independent experiments.

Article Snippet: Searches were performed with a mass measurement tolerance of 10 ppm for precursor ions and 0.02 Da for fragment ions, against a composite target-decoy database constructed using a Msm mc2155 UniProt database (strain ATCC 700084/mc(2)155, taxo 246196, July 20172021, 12666 entries) fused with recombinant trypsin and a list of classical contaminants (118 entries).

Techniques: Construct, Generated, Western Blot, Clone Assay, Transformation Assay

Journal: bioRxiv

Article Title: The cytoplasmic C-terminal domain of the MmpL11 lipid transporter is required for interaction with its co-cistronic partner MSMEG_0240 in Mycobacterium smegmatis

doi: 10.64898/2026.01.19.699910

Figure Lengend Snippet: (A) Schematic representation of the different constructs generated in this study. (B) Western blot analysis using anti-Myc (left panel) or anti-HA (right panel) antibodies of total lysates from two independent clones of Msm mc²155 transformed with pMV361_ MSMEG_0240 , pMV361_ birA-MSMEG_0240 or pMV361_ MSMEG_0240-birA . The positions of BirA-MSMEG_0240 (60 kDa) and MSMEG_0240-BirA (60 kDa) are indicated by the short horizontal bars. (C) OD600nm values at 16 and 40 h from cultures of Msm mc²155 transformed with pMV361_ birA (in black), pMV361_ MSMEG_0240 (in red), pMV361_ birA-MSMEG_0240 (in green) or pMV361_ MSMEG_0240-birA (in blue). (D) Western blot analysis using HRP-conjugated streptavidin of biotinylated proteins from total lysates of Msm mc²155 transformed with pMV361_ birA , pMV361_ MSMEG_0240 , pMV361_ birA-MSMEG_0240 or pMV361_ MSMEG_0240-birA , after enrichment on streptavidin beads. The molecular size markers (M) with their respective sizes expressed in kDa are shown on the left. Images are representative of three independent experiments.

Article Snippet: Searches were performed with a mass measurement tolerance of 10 ppm for precursor ions and 0.02 Da for fragment ions, against a composite target-decoy database constructed using a Msm mc2155 UniProt database (strain ATCC 700084/mc(2)155, taxo 246196, July 20172021, 12666 entries) fused with recombinant trypsin and a list of classical contaminants (118 entries).

Techniques: Construct, Generated, Western Blot, Clone Assay, Transformation Assay

Journal: Current Research in Microbial Sciences

Article Title: A plant-derived antimicrobial peptide with multiple mechanisms of action exhibiting antibacterial and antibiofilm activities comparable to or superior to polymyxin B

doi: 10.1016/j.crmicr.2025.100535

Figure Lengend Snippet: Membrane integrity or damage and morphology of E. coli following exposure to various concentrations of the NCR169C 17–38 peptide. (A) E. coli cells were stained with SYTO 9 and PI, and pictures were taken with confocal microscope; scale bar: 10 µm. (B) Cells were treated with the peptide in the absence of fluorescent dyes and imaged using a scanning electron microscope; scale bar: 1 µm. (C) Monitoring of PI uptake in E. coli treated with a series of concentrations of NCR169C 17–38 in Hidex Plate reader. RFU (535/616) = Relative Fluorescence Units (excitation/emission wavelengths). 0.8 µM Polymyxin B (PMB) was used as a control.

Article Snippet: The trimmed samples were aligned to the E. coli ATCC_8739 genome database using STAR ( ) as described by ( ; supplementary Table 37).

Techniques: Membrane, Staining, Microscopy, Fluorescence, Control

Journal: Current Research in Microbial Sciences

Article Title: A plant-derived antimicrobial peptide with multiple mechanisms of action exhibiting antibacterial and antibiofilm activities comparable to or superior to polymyxin B

doi: 10.1016/j.crmicr.2025.100535

Figure Lengend Snippet: In vitro interaction of NCR169C 17–38 , NCR169, NCR169 16–27 and NCR169 17–27 with nucleic acids. (A) Gel retardation assay of 100 ng E. coli genomic DNA incubated with 0, 10, or 100 µM peptide. (B) Same setup as in (A), but using 100 ng E. coli total RNA. (C) Interaction of NCR169C 17–38 with 250 ng circular plasmid DNA at varying concentrations. (D) Real-time monitoring of DNA binding by fluorescence of SYBR Gold–DNA complexes (excitation 490 nm, emission 535 nm). Peptides (10 µM) were added to 100 ng DNA at 0 or 14 min (red arrows); Proteinase K (1 mg/mL) was added at 27 min (black arrow).

Article Snippet: The trimmed samples were aligned to the E. coli ATCC_8739 genome database using STAR ( ) as described by ( ; supplementary Table 37).

Techniques: In Vitro, Electrophoretic Mobility Shift Assay, Incubation, Plasmid Preparation, Binding Assay, Fluorescence

Journal: Current Research in Microbial Sciences

Article Title: A plant-derived antimicrobial peptide with multiple mechanisms of action exhibiting antibacterial and antibiofilm activities comparable to or superior to polymyxin B

doi: 10.1016/j.crmicr.2025.100535

Figure Lengend Snippet: GO enrichment analysis of DEGs in E coli treated with NCR169C 17–38 annotated in three main categories: (A) biological process, (B) molecular function, and (C) cellular component.

Article Snippet: The trimmed samples were aligned to the E. coli ATCC_8739 genome database using STAR ( ) as described by ( ; supplementary Table 37).

Techniques: