ArticleAnnals of clinical microbiology and antimicrobials2017
PknB remains an essential and a conserved target for drug development in susceptible and MDR strains of M. Tuberculosis.
Article in Annals of clinical microbiology and antimicrobials, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 18 citations in OpenAlex.
- Targeting Bacterial Cell Wall Synthesis: Structural Insights and Emerging Therapeutic Strategies.Pharmaceutics · 2026Review
- Design, Synthesis, and In Vitro Evaluation of 4-(Arylchalcogenyl)methyl)-1H-1,2,3-triazol-1-yl-menadione: Exploring Their Potential AgainstPharmaceuticals (Basel, Switzerland) · 2025Article
- Identification of novel single nucleotide variants in the drug resistance mechanism of Mycobacterium tuberculosis isolates by whole-genome analysis.BMC genomics · 2024Article
- In Silico Identification of Possible Inhibitors for Protein Kinase B (PknB) ofMolecules (Basel, Switzerland) · 2021Article
- Probing the Highly Disparate Dual Inhibitory Mechanisms of Novel Quinazoline Derivatives againstMolecules (Basel, Switzerland) · 2020Article
- Potential therapeutic approaches for a sleeping pathogen: tuberculosis a case for bioinorganic chemistry.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Review
- Defeating Antibiotic-Resistant Bacteria: Exploring Alternative Therapies for a Post-Antibiotic Era.International journal of molecular sciences · 2020Review
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Authors and funding
14 authors at 5 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundThe Mycobacterium tuberculosis (M.tb) protein kinase B (PknB) which is now proved to be essential for the growth and survival of M.tb, is a transmembrane protein with a potential to be a good drug target. However it is not known if this target remains conserved in otherwise resistant isolates from clinical origin. The present study describes the conservation analysis of sequences covering the inhibitor binding domain of PknB to assess if it remains conserved in susceptible and resistant clinical strains of mycobacteria picked from three different geographical areas of India.
methodsA total of 116 isolates from North, South and West India were used in the study with a variable profile of their susceptibilities towards streptomycin, isoniazid, rifampicin, ethambutol and ofloxacin. Isolates were also spoligotyped in order to find if the conservation pattern of pknB gene remain consistent or differ with different spoligotypes. The impact of variation as found in the study was analyzed using Molecular dynamics simulations.
resultsThe sequencing results with 115/116 isolates revealed the conserved nature of pknB sequences irrespective of their susceptibility status and spoligotypes. The only variation found was in one strains wherein pnkB sequence had G to A mutation at 664 position translating into a change of amino acid, Valine to Isoleucine. After analyzing the impact of this sequence variation using Molecular dynamics simulations, it was observed that the variation is causing no significant change in protein structure or the inhibitor binding.
conclusionsHence, the study endorses that PknB is an ideal target for drug development and there is no pre-existing or induced resistance with respect to the sequences involved in inhibitor binding. Also if the mutation that we are reporting for the first time is found again in subsequent work, it should be checked with phenotypic profile before drawing the conclusion that it would affect the activity in any way. Bioinformatics analysis in our study says that it has no significant effect on the binding and hence the activity of the protein.
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