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wild type m pneumoniae strain m129 b7 (ATCC)

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ATCC wild type m pneumoniae strain m129 b7
Wild Type M Pneumoniae Strain M129 B7, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 513 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 96 stars, based on 513 article reviews

wild type m pneumoniae strain m129 b7 - by Bioz Stars, 2026-05

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Sensitivity of the LAMP reaction for the detection of S. pneumoniae , S. aureus , H. influenzae , and M. pneumoniae. Visual LoD determined for the detection of S. pneumoniae (3.9 ×10 3 CFU/mL), S. aureus (1.7 ×10 5 CFU/mL), H. influenzae (8.2 ×10 3 CFU/mL), and M. pneumoniae (1.27 ×10 3 genome copies/reaction) (A) . Verification of amplification by 2% agarose gel electrophoresis (B) .

Journal: Frontiers in Microbiology

Article Title: Development and optimization of an easy to interpret loop-mediated isothermal amplification (LAMP) assay for the identification of bacterial pathogens causing childhood pneumonia

doi: 10.3389/fmicb.2026.1748456

Figure Lengend Snippet: Sensitivity of the LAMP reaction for the detection of S. pneumoniae , S. aureus , H. influenzae , and M. pneumoniae. Visual LoD determined for the detection of S. pneumoniae (3.9 ×10 3 CFU/mL), S. aureus (1.7 ×10 5 CFU/mL), H. influenzae (8.2 ×10 3 CFU/mL), and M. pneumoniae (1.27 ×10 3 genome copies/reaction) (A) . Verification of amplification by 2% agarose gel electrophoresis (B) .

Article Snippet: Initially, tests included panel bacteria: S. pneumoniae ATCC 49619, S. aureus ATCC 25923, H. influenzae ATCC 49766, and purified DNA from M. pneumoniae (ATCC 29342DQ).

Techniques: Amplification, Agarose Gel Electrophoresis

Sensitivity of the designed primers for the detection of K. pneumoniae. Visual LoD (A) . The calculated LoD was 1.5 ×10 4 CFU/mL. Amplification was confirmed by 2% agarose gel electrophoresis (B) .

Journal: Frontiers in Microbiology

Article Title: Development and optimization of an easy to interpret loop-mediated isothermal amplification (LAMP) assay for the identification of bacterial pathogens causing childhood pneumonia

doi: 10.3389/fmicb.2026.1748456

Figure Lengend Snippet: Sensitivity of the designed primers for the detection of K. pneumoniae. Visual LoD (A) . The calculated LoD was 1.5 ×10 4 CFU/mL. Amplification was confirmed by 2% agarose gel electrophoresis (B) .

Article Snippet: Initially, tests included panel bacteria: S. pneumoniae ATCC 49619, S. aureus ATCC 25923, H. influenzae ATCC 49766, and purified DNA from M. pneumoniae (ATCC 29342DQ).

Techniques: Amplification, Agarose Gel Electrophoresis

Relationship between time to positivity and bacterial load for LAMP detection of S. pneumoniae , S. aureus , and H. influenzae . As the bacterial concentration decreased, the time required for detection increased across all three pathogens. For S. pneumoniae , high concentrations produced a clear positive result within 35 min. However, concentrations near the LoD (10 4 and 10 3 CFU/mL) required more than 55 min to be considered positive. Similarly, S. aureus showed a positive signal at 35 min when tested at high concentrations, whereas lower concentrations (around 10 4 CFU/mL) required over 45. In the case of H. influenzae , the highest concentration yielded a visible positive reaction at 25 min, while lower concentrations needed up to 45 min. Transition phase: In all cases, there was a stage where tubes began to show a greenish signal, indicating the onset of positivity, although the color had not yet fully developed to a strong green signal.

Journal: Frontiers in Microbiology

Article Title: Development and optimization of an easy to interpret loop-mediated isothermal amplification (LAMP) assay for the identification of bacterial pathogens causing childhood pneumonia

doi: 10.3389/fmicb.2026.1748456

Figure Lengend Snippet: Relationship between time to positivity and bacterial load for LAMP detection of S. pneumoniae , S. aureus , and H. influenzae . As the bacterial concentration decreased, the time required for detection increased across all three pathogens. For S. pneumoniae , high concentrations produced a clear positive result within 35 min. However, concentrations near the LoD (10 4 and 10 3 CFU/mL) required more than 55 min to be considered positive. Similarly, S. aureus showed a positive signal at 35 min when tested at high concentrations, whereas lower concentrations (around 10 4 CFU/mL) required over 45. In the case of H. influenzae , the highest concentration yielded a visible positive reaction at 25 min, while lower concentrations needed up to 45 min. Transition phase: In all cases, there was a stage where tubes began to show a greenish signal, indicating the onset of positivity, although the color had not yet fully developed to a strong green signal.

Article Snippet: Initially, tests included panel bacteria: S. pneumoniae ATCC 49619, S. aureus ATCC 25923, H. influenzae ATCC 49766, and purified DNA from M. pneumoniae (ATCC 29342DQ).

Techniques: Concentration Assay, Produced

a Graphical representation of the antibiofilm payloads secreted by M. pneumoniae strain CV8_HAD. b Western blot analysis of CV8_HAD lysate and supernatant (SN) showing expression of the payloads; the CV8 chassis and the loaded ribosomal protein RL7 were used as controls. c Representative images of crystal violet assays used to quantify S. aureus (strain Sa15981) or P. aeruginosa (strain PAO1) biofilms after treating with SN from CV8 strains. CV8_D expresses payload D only; CV8_HA expresses payloads H and A. d Plot showing the quantification of biofilm dissolution by CV8 strains SN treatments in vitro, using the crystal violet assay. Data are shown as the mean of three independent experiments ± SEM. *** p < 0.001, ****p < 0.0001 by one-way Anova followed by the post-hoc Tukey’s multiple comparison tests.

Journal: NPJ Biofilms and Microbiomes

Article Title: Engineered Mycoplasma pneumoniae targeting dual-species bacterial biofilms: a novel strategy against infections

doi: 10.1038/s41522-025-00835-2

Figure Lengend Snippet: a Graphical representation of the antibiofilm payloads secreted by M. pneumoniae strain CV8_HAD. b Western blot analysis of CV8_HAD lysate and supernatant (SN) showing expression of the payloads; the CV8 chassis and the loaded ribosomal protein RL7 were used as controls. c Representative images of crystal violet assays used to quantify S. aureus (strain Sa15981) or P. aeruginosa (strain PAO1) biofilms after treating with SN from CV8 strains. CV8_D expresses payload D only; CV8_HA expresses payloads H and A. d Plot showing the quantification of biofilm dissolution by CV8 strains SN treatments in vitro, using the crystal violet assay. Data are shown as the mean of three independent experiments ± SEM. *** p < 0.001, ****p < 0.0001 by one-way Anova followed by the post-hoc Tukey’s multiple comparison tests.

Article Snippet: The attenuated strain CV8 derives from the wild-type M. pneumoniae strain M129 (ATCC 29342, subtype 1), in which genes mpn133 and mpn372 were deleted, and the mpn051 gene was replaced by the gpsA gene from Mycoplasma penetrans .

Techniques: Western Blot, Expressing, Dissolution, In Vitro, Crystal Violet Assay, Comparison

Comparisons of the minimum inhibitory concentrations (MICs) of five antibiotics against M. pneumoniae isolates from five different regions across China during the 2023 epidemic. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001.

Journal: JAC-Antimicrobial Resistance

Article Title: In vitro antimicrobial susceptibility of Mycoplasma pneumoniae isolates across different regions of China in 2023

doi: 10.1093/jacamr/dlaf124

Figure Lengend Snippet: Comparisons of the minimum inhibitory concentrations (MICs) of five antibiotics against M. pneumoniae isolates from five different regions across China during the 2023 epidemic. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001.

Article Snippet: Reference strain M. pneumoniae M129 (ATCC 29342) was used as the macrolide-susceptible control.

Techniques:

Comparisons of the minimum inhibitory concentrations (MICs) of five antibiotics against M. pneumoniae isolates from 10 different provinces/municipalities across China during the 2023 epidemic. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001.

Journal: JAC-Antimicrobial Resistance

Article Title: In vitro antimicrobial susceptibility of Mycoplasma pneumoniae isolates across different regions of China in 2023

doi: 10.1093/jacamr/dlaf124

Figure Lengend Snippet: Comparisons of the minimum inhibitory concentrations (MICs) of five antibiotics against M. pneumoniae isolates from 10 different provinces/municipalities across China during the 2023 epidemic. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001.

Article Snippet: Reference strain M. pneumoniae M129 (ATCC 29342) was used as the macrolide-susceptible control.

Techniques:

(A) Central tomographic slice of a M. pneumoniae cell. Yellow arrowheads indicate the extracellular dome-like complex. Insets show side- and top-views of the complex. The attachment organelle (AO) is indicated. (B) Histogram of particles per cell/tomogram (for 355 tomograms). Indicated are the mean ± standard deviation (SD). (C) Histogram of the percentage of particles observed in clusters of a given size. Particles are defined as being in the same cluster if the center-to-center distance is within 1.3 times the diameter of the particle. (D) Cryo-ET consensus map of the dome complex. The two lines indicate the membrane leaflets and the transmembrane (TM) region between them. The asterisk indicates density that breaks the three-fold symmetry and the triangle indicates the position of the pseudo-symmetry axis. (E) Enlarged view of the area indicated in (D), showing the two large transmembrane regions of the complex: the central (green) and symmetry-breaking (beige) densities. (F-G) The first (F) and second (G) minor transmembrane densities. (H) The cytosolic density of the complex. See also Figure S1.

Journal: bioRxiv

Article Title: In-cell discovery and characterization of a non-canonical bacterial protein translocation-folding complex

doi: 10.1101/2025.04.25.650208

Figure Lengend Snippet: (A) Central tomographic slice of a M. pneumoniae cell. Yellow arrowheads indicate the extracellular dome-like complex. Insets show side- and top-views of the complex. The attachment organelle (AO) is indicated. (B) Histogram of particles per cell/tomogram (for 355 tomograms). Indicated are the mean ± standard deviation (SD). (C) Histogram of the percentage of particles observed in clusters of a given size. Particles are defined as being in the same cluster if the center-to-center distance is within 1.3 times the diameter of the particle. (D) Cryo-ET consensus map of the dome complex. The two lines indicate the membrane leaflets and the transmembrane (TM) region between them. The asterisk indicates density that breaks the three-fold symmetry and the triangle indicates the position of the pseudo-symmetry axis. (E) Enlarged view of the area indicated in (D), showing the two large transmembrane regions of the complex: the central (green) and symmetry-breaking (beige) densities. (F-G) The first (F) and second (G) minor transmembrane densities. (H) The cytosolic density of the complex. See also Figure S1.

Article Snippet: The AlphaFold2 predicated models for the whole proteome of M. pneumoniae strain M129 (ATCC 29342) were downloaded from the AlphaFold Database ( https://alphafold.ebi.ac.uk , accessed during July 2022).

Techniques: Standard Deviation, Tomography, Membrane

(A) Workflow for determining homology of Mdps: structural domains of the Mdps were determined and excised from the AlphaFold2 predictions. These domains were used to perform structure-based homology searches using DALI and FoldSeek. Shown is the Mdp444 N-ter SurA domain (teal) aligned to pdb: 6VJ4 (grey), the N-ter PPIC domain (salmon) aligned to afdb: AF-A0A3M6KDR7-F1-v4 (grey), the C-ter SurA domain (blue) aligned to pdb: 5HTF (grey), and the C-ter PPIC domain (pink) aligned to afdb: AF-A0A5C6BMD5 (grey). (B) The domain arrangement determined from the structural homology searches shows that all three Mdps have an N- and C-terminal structural unit both consisting of a SurA domain followed by a PPIC domain. The white boxes indicate insertions. (C) Superposition of SurA domain from the Mdp444 N-terminal SurA domain (teal) and PrsA from Bacillus anthracis (pdb 6VJ4; grey). (D) The PPIC domain from Bacillus subtilis PrsA (pdb 1ZK6; grey) with the residues important for catalytic function indicated in bold, and the residues important for substrate binding indicated in regular text. The corresponding residues are indicated on the N-terminal PPIC domain of Mdp444, followed by a superposition of the two, showing that the catalytic and substrate binding residues are conserved. (E-F) A reconciliated phylogenetic tree, showing the evolutionary events of (E) the Mdp family of proteins, and (F) MPN523 in Mycoplasma , and other bacteria. The black outline indicates the species tree, and the colored lines indicate the proteins. The lines are colored to indicate whether (E) the catalytic residues are conserved (orange) or not (blue) for the Mdps, or (F) whether the CXXC motif is conserved (yellow) or not (green). The sequence similarity and alignment length of all M. pneumoniae paralogs of the Mdps is shown in Figure S2E-F. See also Figure S3.

Journal: bioRxiv

Article Title: In-cell discovery and characterization of a non-canonical bacterial protein translocation-folding complex

doi: 10.1101/2025.04.25.650208

Figure Lengend Snippet: (A) Workflow for determining homology of Mdps: structural domains of the Mdps were determined and excised from the AlphaFold2 predictions. These domains were used to perform structure-based homology searches using DALI and FoldSeek. Shown is the Mdp444 N-ter SurA domain (teal) aligned to pdb: 6VJ4 (grey), the N-ter PPIC domain (salmon) aligned to afdb: AF-A0A3M6KDR7-F1-v4 (grey), the C-ter SurA domain (blue) aligned to pdb: 5HTF (grey), and the C-ter PPIC domain (pink) aligned to afdb: AF-A0A5C6BMD5 (grey). (B) The domain arrangement determined from the structural homology searches shows that all three Mdps have an N- and C-terminal structural unit both consisting of a SurA domain followed by a PPIC domain. The white boxes indicate insertions. (C) Superposition of SurA domain from the Mdp444 N-terminal SurA domain (teal) and PrsA from Bacillus anthracis (pdb 6VJ4; grey). (D) The PPIC domain from Bacillus subtilis PrsA (pdb 1ZK6; grey) with the residues important for catalytic function indicated in bold, and the residues important for substrate binding indicated in regular text. The corresponding residues are indicated on the N-terminal PPIC domain of Mdp444, followed by a superposition of the two, showing that the catalytic and substrate binding residues are conserved. (E-F) A reconciliated phylogenetic tree, showing the evolutionary events of (E) the Mdp family of proteins, and (F) MPN523 in Mycoplasma , and other bacteria. The black outline indicates the species tree, and the colored lines indicate the proteins. The lines are colored to indicate whether (E) the catalytic residues are conserved (orange) or not (blue) for the Mdps, or (F) whether the CXXC motif is conserved (yellow) or not (green). The sequence similarity and alignment length of all M. pneumoniae paralogs of the Mdps is shown in Figure S2E-F. See also Figure S3.

Techniques: Binding Assay, Bacteria, Sequencing

(A) Tomographic slice of a M. pneumoniae cell showing a ribosome (blue arrowhead), the plasma membrane (PM) and the dome complexes (yellow arrowheads) on the cell surface. (B) Nearest neighbor analysis, showing the distance for each dome complex to the nearest ribosome in untreated cells and in cells treated with pseudouridimycin (PUM) or chloramphenicol (Cm). The distance was measured from SecA to the peptide exit site. (C-E) Cryo-ET maps of the dome-ribosome supercomplex resolved in untreated cells (C), or antibiotics-treated cells (D) and the corresponding structural model (E). (F) View of the nascent peptide density extending from the ribosome peptidyl transfer center to the exit site (yellow). Low density thresholding was used to visualize the substrate density inside the dome cavity (blue asterisk). (G-J) Model fitting of SecA (G), SecDF-SecYEG (H-I) and the Mdps (J) in the multibody derived maps. See also Figures S5 and S6.

Journal: bioRxiv

Article Title: In-cell discovery and characterization of a non-canonical bacterial protein translocation-folding complex

doi: 10.1101/2025.04.25.650208

Figure Lengend Snippet: (A) Tomographic slice of a M. pneumoniae cell showing a ribosome (blue arrowhead), the plasma membrane (PM) and the dome complexes (yellow arrowheads) on the cell surface. (B) Nearest neighbor analysis, showing the distance for each dome complex to the nearest ribosome in untreated cells and in cells treated with pseudouridimycin (PUM) or chloramphenicol (Cm). The distance was measured from SecA to the peptide exit site. (C-E) Cryo-ET maps of the dome-ribosome supercomplex resolved in untreated cells (C), or antibiotics-treated cells (D) and the corresponding structural model (E). (F) View of the nascent peptide density extending from the ribosome peptidyl transfer center to the exit site (yellow). Low density thresholding was used to visualize the substrate density inside the dome cavity (blue asterisk). (G-J) Model fitting of SecA (G), SecDF-SecYEG (H-I) and the Mdps (J) in the multibody derived maps. See also Figures S5 and S6.

Techniques: Clinical Proteomics, Membrane, Tomography, Derivative Assay

(A) Schematic model of the translocation cycle in M. pneumoniae . SecA binding primes the complex for translocation, involving reorganization of the SecDF-SecYEG architecture, and interactions with the extracellular dome proteins. (B) Structural models of the different dome-complexes. In the pre-translocation state, the SecA-unbound dome is in a resting state. Association of SecA with a substrate initiates translocaiton. Co-translational translocation can either happen in a flexible form with ribosome and dome associated via the nascent peptide or directly through physical coupling of the two macromolecular complexes, forming a supercomplex.

Journal: bioRxiv

Article Title: In-cell discovery and characterization of a non-canonical bacterial protein translocation-folding complex

doi: 10.1101/2025.04.25.650208

Figure Lengend Snippet: (A) Schematic model of the translocation cycle in M. pneumoniae . SecA binding primes the complex for translocation, involving reorganization of the SecDF-SecYEG architecture, and interactions with the extracellular dome proteins. (B) Structural models of the different dome-complexes. In the pre-translocation state, the SecA-unbound dome is in a resting state. Association of SecA with a substrate initiates translocaiton. Co-translational translocation can either happen in a flexible form with ribosome and dome associated via the nascent peptide or directly through physical coupling of the two macromolecular complexes, forming a supercomplex.

Techniques: Translocation Assay, Binding Assay

Bioinformatics Analysis of M. pneumoniae P1C1079–1518. (A) Prediction of the secondary structure features of P1C1079–1518. (B) Prediction of the tertiary structure of P1C1079–1518. (C) Minimum free energy (MFE) secondary structure of mRNA encoding P1C1079–1518. (D) Centroid secondary structure of mRNA encoding P1C1079–1518.

Journal: Microbiology Spectrum

Article Title: Protective immunity induced by a novel P1 adhesin C-terminal anchored mRNA vaccine against Mycoplasma pneumoniae infection in BALB/c mice

doi: 10.1128/spectrum.02140-24

Figure Lengend Snippet: Bioinformatics Analysis of M. pneumoniae P1C1079–1518. (A) Prediction of the secondary structure features of P1C1079–1518. (B) Prediction of the tertiary structure of P1C1079–1518. (C) Minimum free energy (MFE) secondary structure of mRNA encoding P1C1079–1518. (D) Centroid secondary structure of mRNA encoding P1C1079–1518.

Article Snippet: The M. pneumoniae M129 strain (ATCC 29342) used in this study is maintained at the Institute of Pathogenic Biology, University of South China.

Techniques:

Construction, expression, purification, and identification of pET-28a(+)/RP1C1079–1518. (A) 0.8% agarose gel electrophoresis: Lane 1 shows the double digestion electrophoresis, and Lane 2 shows the original plasmid electrophoresis. (B) Coomassie brilliant blue analysis of RP1C1079–1518 separated by 12.5% SDS-PAGE: Lanes 1–9 represent RP1C 1079–1518 eluted with 80 mM imidazole wash buffer, with an expected size of approximately 47 kDa. (C) Western blot analysis of M. pneumoniae RP1C 1079–1518 using anti- M . pneumoniae antibody. (D). Western blot analysis of M. pneumoniae RP1C 1079–1518 using anti-His antibody.

Journal: Microbiology Spectrum

Article Title: Protective immunity induced by a novel P1 adhesin C-terminal anchored mRNA vaccine against Mycoplasma pneumoniae infection in BALB/c mice

doi: 10.1128/spectrum.02140-24

Figure Lengend Snippet: Construction, expression, purification, and identification of pET-28a(+)/RP1C1079–1518. (A) 0.8% agarose gel electrophoresis: Lane 1 shows the double digestion electrophoresis, and Lane 2 shows the original plasmid electrophoresis. (B) Coomassie brilliant blue analysis of RP1C1079–1518 separated by 12.5% SDS-PAGE: Lanes 1–9 represent RP1C 1079–1518 eluted with 80 mM imidazole wash buffer, with an expected size of approximately 47 kDa. (C) Western blot analysis of M. pneumoniae RP1C 1079–1518 using anti- M . pneumoniae antibody. (D). Western blot analysis of M. pneumoniae RP1C 1079–1518 using anti-His antibody.

Article Snippet: The M. pneumoniae M129 strain (ATCC 29342) used in this study is maintained at the Institute of Pathogenic Biology, University of South China.

Techniques: Expressing, Purification, Agarose Gel Electrophoresis, Electrophoresis, Plasmid Preparation, SDS Page, Western Blot

Detection of lung tissue changes in mice on the 7th day post M. pneumoniae challenge. (A) Unstained and Dienes-Stained M. pneumoniae on PPLO Agar. (B) H&E-stained lung tissue sections of mice from different groups post M. pneumoniae challenge. (C) Pathology score of lung tissue sections from mice. (D) M. pneumoniae DNA load in lung tissue homogenates of mice. (E) M. pneumoniae DNA copy numbers. Data are presented as mean ± 95% CI. Statistical significance tested by one-way ANOVA test (* P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001).

Journal: Microbiology Spectrum

Article Title: Protective immunity induced by a novel P1 adhesin C-terminal anchored mRNA vaccine against Mycoplasma pneumoniae infection in BALB/c mice

doi: 10.1128/spectrum.02140-24

Figure Lengend Snippet: Detection of lung tissue changes in mice on the 7th day post M. pneumoniae challenge. (A) Unstained and Dienes-Stained M. pneumoniae on PPLO Agar. (B) H&E-stained lung tissue sections of mice from different groups post M. pneumoniae challenge. (C) Pathology score of lung tissue sections from mice. (D) M. pneumoniae DNA load in lung tissue homogenates of mice. (E) M. pneumoniae DNA copy numbers. Data are presented as mean ± 95% CI. Statistical significance tested by one-way ANOVA test (* P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001).

Article Snippet: The M. pneumoniae M129 strain (ATCC 29342) used in this study is maintained at the Institute of Pathogenic Biology, University of South China.

Techniques: Staining

Cytokine detection in lung tissue homogenate supernatants post- M. pneumoniae challenge. (A) Detection of IL-6 in lung tissue homogenate supernatants. (B) Detection of IL-4 in lung tissue homogenate supernatants. (C) Detection of IFN-γ in lung tissue homogenate supernatants. (D) Detection of IL-10 in lung tissue homogenate supernatants. Data are presented as mean ± 95% CI. Statistical significance tested by one-way ANOVA test (* P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001).

Journal: Microbiology Spectrum

Article Title: Protective immunity induced by a novel P1 adhesin C-terminal anchored mRNA vaccine against Mycoplasma pneumoniae infection in BALB/c mice

doi: 10.1128/spectrum.02140-24

Figure Lengend Snippet: Cytokine detection in lung tissue homogenate supernatants post- M. pneumoniae challenge. (A) Detection of IL-6 in lung tissue homogenate supernatants. (B) Detection of IL-4 in lung tissue homogenate supernatants. (C) Detection of IFN-γ in lung tissue homogenate supernatants. (D) Detection of IL-10 in lung tissue homogenate supernatants. Data are presented as mean ± 95% CI. Statistical significance tested by one-way ANOVA test (* P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001).

Article Snippet: The M. pneumoniae M129 strain (ATCC 29342) used in this study is maintained at the Institute of Pathogenic Biology, University of South China.

Techniques:

Journal: Microbiology Spectrum

Article Title: Protective immunity induced by a novel P1 adhesin C-terminal anchored mRNA vaccine against Mycoplasma pneumoniae infection in BALB/c mice

doi: 10.1128/spectrum.02140-24

Article Snippet: The genomic DNA of the M. pneumoniae M129 standard strain (ATCC 29342) was used as a template to design primers.

Techniques:

Journal: Microbiology Spectrum

Article Title: Protective immunity induced by a novel P1 adhesin C-terminal anchored mRNA vaccine against Mycoplasma pneumoniae infection in BALB/c mice

doi: 10.1128/spectrum.02140-24

Article Snippet: The genomic DNA of the M. pneumoniae M129 standard strain (ATCC 29342) was used as a template to design primers.

Techniques: Expressing, Purification, Agarose Gel Electrophoresis, Electrophoresis, Plasmid Preparation, SDS Page, Western Blot

Journal: Microbiology Spectrum

Article Title: Protective immunity induced by a novel P1 adhesin C-terminal anchored mRNA vaccine against Mycoplasma pneumoniae infection in BALB/c mice

doi: 10.1128/spectrum.02140-24

Article Snippet: The genomic DNA of the M. pneumoniae M129 standard strain (ATCC 29342) was used as a template to design primers.

Techniques: Staining

Journal: Microbiology Spectrum

Article Title: Protective immunity induced by a novel P1 adhesin C-terminal anchored mRNA vaccine against Mycoplasma pneumoniae infection in BALB/c mice

doi: 10.1128/spectrum.02140-24

Article Snippet: The genomic DNA of the M. pneumoniae M129 standard strain (ATCC 29342) was used as a template to design primers.

Techniques:

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