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k pneumoniae atcc baa  (ATCC)


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    Structured Review

    ATCC k pneumoniae atcc baa
    K Pneumoniae Atcc Baa, supplied by ATCC, used in various techniques. Bioz Stars score: 98/100, based on 434 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/k+pneumoniae+atcc+baa+2146/Klebsiella+pneumoniae+(Schroeter)+Trevisan/pm42770986-27-34-36
    Average 98 stars, based on 434 article reviews
    k pneumoniae atcc baa - by Bioz Stars, 2026-11
    98/100 stars

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    Related Articles

    Transformation Assay:

    Article Title: Rational Design of 1H-pyrrole-2-carboxylic Acid Inhibitors of NDM-1 Metallo-β-lactamase Restoring β-Lactam Efficacy Against Resistant Enterobacterales
    Article Snippet: Antimicrobial resistance mediated by metallo-β-lactamases (MBLs) represents a critical challenge for the efficacy of β-lactam antibiotics.. Here, we report the design, synthesis, and evaluation of a novel class of 3,5-diaryl-1Hpyrrole-2-carboxylic acids as potent New Delhi metallo-β-lactamase (NDM)-type MBL inhibitors.. Guided by molecular modeling and structure–activity relationship studies, the pyrrole scaffold was optimized through systematic modifications of the phenyl rings at position 3 and 5 of pyrrole core, yielding derivatives with lownanomolar IC50 values against NDM-1.

    Plasmid Preparation:

    Article Title: Rational Design of 1H-pyrrole-2-carboxylic Acid Inhibitors of NDM-1 Metallo-β-lactamase Restoring β-Lactam Efficacy Against Resistant Enterobacterales
    Article Snippet: Antimicrobial resistance mediated by metallo-β-lactamases (MBLs) represents a critical challenge for the efficacy of β-lactam antibiotics.. Here, we report the design, synthesis, and evaluation of a novel class of 3,5-diaryl-1Hpyrrole-2-carboxylic acids as potent New Delhi metallo-β-lactamase (NDM)-type MBL inhibitors.. Guided by molecular modeling and structure–activity relationship studies, the pyrrole scaffold was optimized through systematic modifications of the phenyl rings at position 3 and 5 of pyrrole core, yielding derivatives with lownanomolar IC50 values against NDM-1.

    Mutagenesis:

    Article Title: Peptoid-based antimicrobial strategies against polymyxin-resistant Gram-negative bacteria.
    Article Snippet: .. Similarly, another study on a colistin-resistant mutant of K. pneumoniae ATCC BAA 2146 identified a ccrB missense mutation encoding the HAMP domain-containing histidine kinase CrrB, together with a silent satP mutation (Sun et al. 2020), suggesting possible alterations in two-component regulatory signaling. ..

    Article Title: PhoP-regulated VirK acts as an accessory factor to maintain virulence in polymyxin-resistant Klebsiella pneumoniae
    Article Snippet: .. During preliminary investigations of a polymyxin-resistant mutant (Mut-S) of K. pneumoniae ATCC BAA-2146 (Kpn2146) [ ], we detected highly upregulated expression of the Kpn2146:RS17285 gene. ..

    Article Title: Peptoid-based antimicrobial strategies against polymyxin-resistant Gram-negative bacteria
    Article Snippet: .. Similarly, another study on a colistin-resistant mutant of K. pneumoniae ATCC BAA 2146 identified a ccrB missense mutation encoding the HAMP domain-containing histidine kinase CrrB, together with a silent satP mutation (Sun et al. ), suggesting possible alterations in two-component regulatory signaling. ..

    Expressing:

    Article Title: PhoP-regulated VirK acts as an accessory factor to maintain virulence in polymyxin-resistant Klebsiella pneumoniae
    Article Snippet: .. During preliminary investigations of a polymyxin-resistant mutant (Mut-S) of K. pneumoniae ATCC BAA-2146 (Kpn2146) [ ], we detected highly upregulated expression of the Kpn2146:RS17285 gene. ..

    Control:




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    k pneumoniae atcc baa  (ATCC)
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    k pneumoniae atcc baa 2146  (ATCC)
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    k pneumoniae atcc baa2146  (ATCC)
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    ATCC k pneumoniae atcc baa2146
    Sequence and structure comparison of VirK (from K. pneumoniae ATCC <t>BAA2146)</t> and YbjX (from E. coli K-12 ) proteins. ( A ) Alignment of the amino acid sequence of VirK ( Q ) with that of YbjX ( T ); ( B ) Comparison of the protein structures of VirK and YbjX. Amino acid sequences and structures were compared using the foldseek server . The protein structure of YbjX was obtained from the AFDB database (AFDB accession: AF- P75829 -F1).
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    k pneumoniae atcc baa2146 serial strains  (ATCC)
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    ATCC k pneumoniae atcc baa2146 serial strains
    Sequence and structure comparison of VirK (from K. pneumoniae ATCC <t>BAA2146)</t> and YbjX (from E. coli K-12 ) proteins. ( A ) Alignment of the amino acid sequence of VirK ( Q ) with that of YbjX ( T ); ( B ) Comparison of the protein structures of VirK and YbjX. Amino acid sequences and structures were compared using the foldseek server . The protein structure of YbjX was obtained from the AFDB database (AFDB accession: AF- P75829 -F1).
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    k pneumoniae atcc baa 2146 genome  (ATCC)
    98
    ATCC k pneumoniae atcc baa 2146 genome
    PhoP directly regulates the expression of virK in K. pneumoniae . ( A ) The ability of PhoP to bind to the virK promoter was determined by EMSA. His-tagged PhoP was incubated with virK and 16S rDNA (negative control) in a concentration gradient. The experiments were repeated three times. An upward arrow marks bound DNA fragments, a middle arrow indicates free DNA fragments, and the bottom arrow represents the 16S rDNA fragment.( B ) Mapping of PhoP binding sites in K. pneumoniae ATCC <t>BAA</t> <t>2146</t> by ChIP-seq. IGV genome browser view showing PhoP binding regions around the virK gene across the K. pneumoniae genome. IP: Experimental group, namely the IP samples; IN: Control group, namely the IN sample; numbers represent three independent replicate trials. ( C ) ChIP and real-time PCR assays were used to investigate the binding of PhoP to the putative binding site in the promoter region of the virK gene. The experiments were independently repeated three times. The PhoQ gene was used as a positive control. The ChIP DNA was enriched using an IgG antibody and a Flag antibody and quantified by qPCR. ( D ) DNase I footprinting analysis of PhoP binding to the virK promoter. The intergenic fragment was labeled with 6-carboxyfluorescein (FAM) dye and incubated with 10 μg of PhoP (upper curve) or without PhoP (lower curve). The region protected by PhoP from DNase I cleavage is indicated with a black dotted box (ACACCTCAATCAATTTTAA).
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    Average 98 stars, based on 1 article reviews
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    Image Search Results


    Sequence and structure comparison of VirK (from K. pneumoniae ATCC BAA2146) and YbjX (from E. coli K-12 ) proteins. ( A ) Alignment of the amino acid sequence of VirK ( Q ) with that of YbjX ( T ); ( B ) Comparison of the protein structures of VirK and YbjX. Amino acid sequences and structures were compared using the foldseek server . The protein structure of YbjX was obtained from the AFDB database (AFDB accession: AF- P75829 -F1).

    Journal: Nucleic Acids Research

    Article Title: PhoP-regulated VirK acts as an accessory factor to maintain virulence in polymyxin-resistant Klebsiella pneumoniae

    doi: 10.1093/nar/gkag290

    Figure Lengend Snippet: Sequence and structure comparison of VirK (from K. pneumoniae ATCC BAA2146) and YbjX (from E. coli K-12 ) proteins. ( A ) Alignment of the amino acid sequence of VirK ( Q ) with that of YbjX ( T ); ( B ) Comparison of the protein structures of VirK and YbjX. Amino acid sequences and structures were compared using the foldseek server . The protein structure of YbjX was obtained from the AFDB database (AFDB accession: AF- P75829 -F1).

    Article Snippet: The effects of virK on bacterial pathogenicity were further evaluated in a mouse systemic infection model using virK mutants and complemented strains under K. pneumoniae ATCC BAA2146 (wild type) or Mut-S ( mgrB truncated strain) backgrounds.

    Techniques: Sequencing, Comparison

    Sequence and structure comparison of VirK (from K. pneumoniae ATCC BAA2146) and YbjX (from E. coli K-12 ) proteins. ( A ) Alignment of the amino acid sequence of VirK ( Q ) with that of YbjX ( T ); ( B ) Comparison of the protein structures of VirK and YbjX. Amino acid sequences and structures were compared using the foldseek server . The protein structure of YbjX was obtained from the AFDB database (AFDB accession: AF- P75829 -F1).

    Journal: Nucleic Acids Research

    Article Title: PhoP-regulated VirK acts as an accessory factor to maintain virulence in polymyxin-resistant Klebsiella pneumoniae

    doi: 10.1093/nar/gkag290

    Figure Lengend Snippet: Sequence and structure comparison of VirK (from K. pneumoniae ATCC BAA2146) and YbjX (from E. coli K-12 ) proteins. ( A ) Alignment of the amino acid sequence of VirK ( Q ) with that of YbjX ( T ); ( B ) Comparison of the protein structures of VirK and YbjX. Amino acid sequences and structures were compared using the foldseek server . The protein structure of YbjX was obtained from the AFDB database (AFDB accession: AF- P75829 -F1).

    Article Snippet: Results from K. pneumoniae ATCC BAA2146 serial strains suggested that virK deficiency resulted in a modest reduction in bacterial virulence, while complementation partially restored this phenotype.

    Techniques: Sequencing, Comparison

    PhoP directly regulates the expression of virK in K. pneumoniae . ( A ) The ability of PhoP to bind to the virK promoter was determined by EMSA. His-tagged PhoP was incubated with virK and 16S rDNA (negative control) in a concentration gradient. The experiments were repeated three times. An upward arrow marks bound DNA fragments, a middle arrow indicates free DNA fragments, and the bottom arrow represents the 16S rDNA fragment.( B ) Mapping of PhoP binding sites in K. pneumoniae ATCC BAA 2146 by ChIP-seq. IGV genome browser view showing PhoP binding regions around the virK gene across the K. pneumoniae genome. IP: Experimental group, namely the IP samples; IN: Control group, namely the IN sample; numbers represent three independent replicate trials. ( C ) ChIP and real-time PCR assays were used to investigate the binding of PhoP to the putative binding site in the promoter region of the virK gene. The experiments were independently repeated three times. The PhoQ gene was used as a positive control. The ChIP DNA was enriched using an IgG antibody and a Flag antibody and quantified by qPCR. ( D ) DNase I footprinting analysis of PhoP binding to the virK promoter. The intergenic fragment was labeled with 6-carboxyfluorescein (FAM) dye and incubated with 10 μg of PhoP (upper curve) or without PhoP (lower curve). The region protected by PhoP from DNase I cleavage is indicated with a black dotted box (ACACCTCAATCAATTTTAA).

    Journal: Nucleic Acids Research

    Article Title: PhoP-regulated VirK acts as an accessory factor to maintain virulence in polymyxin-resistant Klebsiella pneumoniae

    doi: 10.1093/nar/gkag290

    Figure Lengend Snippet: PhoP directly regulates the expression of virK in K. pneumoniae . ( A ) The ability of PhoP to bind to the virK promoter was determined by EMSA. His-tagged PhoP was incubated with virK and 16S rDNA (negative control) in a concentration gradient. The experiments were repeated three times. An upward arrow marks bound DNA fragments, a middle arrow indicates free DNA fragments, and the bottom arrow represents the 16S rDNA fragment.( B ) Mapping of PhoP binding sites in K. pneumoniae ATCC BAA 2146 by ChIP-seq. IGV genome browser view showing PhoP binding regions around the virK gene across the K. pneumoniae genome. IP: Experimental group, namely the IP samples; IN: Control group, namely the IN sample; numbers represent three independent replicate trials. ( C ) ChIP and real-time PCR assays were used to investigate the binding of PhoP to the putative binding site in the promoter region of the virK gene. The experiments were independently repeated three times. The PhoQ gene was used as a positive control. The ChIP DNA was enriched using an IgG antibody and a Flag antibody and quantified by qPCR. ( D ) DNase I footprinting analysis of PhoP binding to the virK promoter. The intergenic fragment was labeled with 6-carboxyfluorescein (FAM) dye and incubated with 10 μg of PhoP (upper curve) or without PhoP (lower curve). The region protected by PhoP from DNase I cleavage is indicated with a black dotted box (ACACCTCAATCAATTTTAA).

    Article Snippet: Sequence reads were obtained from ChIP-seq analysis using an anti-Flag antibody and mapped to the K. pneumoniae ATCC BAA-2146 genome (ASM36438v3).

    Techniques: Expressing, Incubation, Negative Control, Concentration Assay, Binding Assay, ChIP-sequencing, Control, Real-time Polymerase Chain Reaction, Positive Control, Footprinting, Labeling