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radd  (ATCC)
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ATCC radd
(A) Schematic of the pZP06B plasmid, in which the galK gene was replaced with sacB under the control of the rpsJ promoter, enabling sacB -based counterselection. (B) Schematic of pZP06C, an enhanced version of pZP06B, containing a mCherry reporter cassette in the multiple cloning site (MCS) to provide a visual marker for identifying positive clones. (C) Construction of pZP06CΔradD for deleting the <t>radD</t> gene in Fusobacterium nucleatum strain 21_1A. The radD gene encodes a large surface adhesion protein that facilitates coaggregation with oral bacteria. (D) PCR analysis using primer pair P7/P8 (indicated in panel C) of ten sucrose-resistant colonies after sacB counterselection in four Fusobacterium strains (21_1A, <t>CTI-2,</t> <t>ATCC</t> 10953, and ATCC 23726). In strain 21_1A, four colonies produced a 2.0 kb amplicon, indicating a radD deletion, while the remaining six colonies produced the 8.3 kb wild-type amplicon. In the other strains, the PCR results showed varying numbers of mutants and wild-type colonies, with smaller amplicons corresponding to the radD deletions and larger amplicons corresponding to the wild-type genotype. (E) Coaggregation assays with A. oris MG-1. Deletion of the radD gene abolished coaggregation in strains 21_1A, ATCC 10953, and ATCC 23726 but not in strain CTI-2. The wild-type and ΔradD mutant cells for each strain were cultured in TSPC medium to the stationary phase, then collected, washed, resuspended in coaggregation buffer, and assessed for coaggregation with an equal amount of A. oris cells. Representative results are shown from repeated experiments with all screened mutant colonies. (F) Western blot analysis of RadD expression in wild-type and ΔradD mutant strains. Cells used in the coaggregation assays in panel E underwent SDS-PAGE, followed by immunoblotting. Antibodies specific to RadD (α-RadD) and HsIJ (α-HsIJ) were used for detection, with HsIJ serving as a loading control . Molecular weight markers (in kilodaltons) are indicated on the left side of the blot.
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(A) Schematic of the pZP06B plasmid, in which the galK gene was replaced with sacB under the control of the rpsJ promoter, enabling sacB -based counterselection. (B) Schematic of pZP06C, an enhanced version of pZP06B, containing a mCherry reporter cassette in the multiple cloning site (MCS) to provide a visual marker for identifying positive clones. (C) Construction of pZP06CΔradD for deleting the radD gene in Fusobacterium nucleatum strain 21_1A. The radD gene encodes a large surface adhesion protein that facilitates coaggregation with oral bacteria. (D) PCR analysis using primer pair P7/P8 (indicated in panel C) of ten sucrose-resistant colonies after sacB counterselection in four Fusobacterium strains (21_1A, CTI-2, ATCC 10953, and ATCC 23726). In strain 21_1A, four colonies produced a 2.0 kb amplicon, indicating a radD deletion, while the remaining six colonies produced the 8.3 kb wild-type amplicon. In the other strains, the PCR results showed varying numbers of mutants and wild-type colonies, with smaller amplicons corresponding to the radD deletions and larger amplicons corresponding to the wild-type genotype. (E) Coaggregation assays with A. oris MG-1. Deletion of the radD gene abolished coaggregation in strains 21_1A, ATCC 10953, and ATCC 23726 but not in strain CTI-2. The wild-type and ΔradD mutant cells for each strain were cultured in TSPC medium to the stationary phase, then collected, washed, resuspended in coaggregation buffer, and assessed for coaggregation with an equal amount of A. oris cells. Representative results are shown from repeated experiments with all screened mutant colonies. (F) Western blot analysis of RadD expression in wild-type and ΔradD mutant strains. Cells used in the coaggregation assays in panel E underwent SDS-PAGE, followed by immunoblotting. Antibodies specific to RadD (α-RadD) and HsIJ (α-HsIJ) were used for detection, with HsIJ serving as a loading control . Molecular weight markers (in kilodaltons) are indicated on the left side of the blot.

Journal: bioRxiv

Article Title: Development of a Conditional Plasmid for Gene Deletion in Non-Model Fusobacterium nucleatum strains

doi: 10.1101/2024.09.09.612158

Figure Lengend Snippet: (A) Schematic of the pZP06B plasmid, in which the galK gene was replaced with sacB under the control of the rpsJ promoter, enabling sacB -based counterselection. (B) Schematic of pZP06C, an enhanced version of pZP06B, containing a mCherry reporter cassette in the multiple cloning site (MCS) to provide a visual marker for identifying positive clones. (C) Construction of pZP06CΔradD for deleting the radD gene in Fusobacterium nucleatum strain 21_1A. The radD gene encodes a large surface adhesion protein that facilitates coaggregation with oral bacteria. (D) PCR analysis using primer pair P7/P8 (indicated in panel C) of ten sucrose-resistant colonies after sacB counterselection in four Fusobacterium strains (21_1A, CTI-2, ATCC 10953, and ATCC 23726). In strain 21_1A, four colonies produced a 2.0 kb amplicon, indicating a radD deletion, while the remaining six colonies produced the 8.3 kb wild-type amplicon. In the other strains, the PCR results showed varying numbers of mutants and wild-type colonies, with smaller amplicons corresponding to the radD deletions and larger amplicons corresponding to the wild-type genotype. (E) Coaggregation assays with A. oris MG-1. Deletion of the radD gene abolished coaggregation in strains 21_1A, ATCC 10953, and ATCC 23726 but not in strain CTI-2. The wild-type and ΔradD mutant cells for each strain were cultured in TSPC medium to the stationary phase, then collected, washed, resuspended in coaggregation buffer, and assessed for coaggregation with an equal amount of A. oris cells. Representative results are shown from repeated experiments with all screened mutant colonies. (F) Western blot analysis of RadD expression in wild-type and ΔradD mutant strains. Cells used in the coaggregation assays in panel E underwent SDS-PAGE, followed by immunoblotting. Antibodies specific to RadD (α-RadD) and HsIJ (α-HsIJ) were used for detection, with HsIJ serving as a loading control . Molecular weight markers (in kilodaltons) are indicated on the left side of the blot.

Article Snippet: To improve specificity, we developed a new RadD antibody using a recombinant protein containing amino acids 44-200 of RadD from ATCC 23726, a region highly conserved among RadD homologs (Fig. S1).

Techniques: Plasmid Preparation, Control, Cloning, Marker, Clone Assay, Bacteria, Produced, Amplification, Mutagenesis, Cell Culture, Western Blot, Expressing, SDS Page, Molecular Weight