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  1. Article ; Online: Proteomic Analysis of the

    Palande, Aseem / Patil, Saniya / Veeram, Anjali / Sahoo, Soumya Swastik / Lodhiya, Tejan / Maurya, Pankaj / Muralikrishnan, Balaji / Chugh, Jeetender / Mukherjee, Raju

    ACS infectious diseases

    2024  Volume 10, Issue 3, Page(s) 890–906

    Abstract: Increased resistance to current antimycobacterial agents and a potential bias toward relatively hydrophobic chemical entities highlight an urgent need to understand how current anti-TB drugs enter the tubercle bacilli. While inner membrane proteins are ... ...

    Abstract Increased resistance to current antimycobacterial agents and a potential bias toward relatively hydrophobic chemical entities highlight an urgent need to understand how current anti-TB drugs enter the tubercle bacilli. While inner membrane proteins are well-studied, how small molecules cross the impenetrable outer membrane remains unknown. Here, we employed mass spectrometry-based proteomics to show that octyl-β-d-glucopyranoside selectively extracts the outer membrane proteins of
    MeSH term(s) Humans ; Mycobacterium tuberculosis/genetics ; Mycobacterium tuberculosis/metabolism ; Proteomics ; Tuberculosis/microbiology ; Anti-Bacterial Agents/metabolism ; Membrane Proteins/metabolism
    Chemical Substances Anti-Bacterial Agents ; Membrane Proteins
    Language English
    Publishing date 2024-02-24
    Publishing country United States
    Document type Journal Article
    ISSN 2373-8227
    ISSN (online) 2373-8227
    DOI 10.1021/acsinfecdis.3c00517
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Overexpression of a membrane transport system MSMEG_1381 and MSMEG_1382 confers multidrug resistance in Mycobacterium smegmatis.

    Salini, S / Muralikrishnan, Balaji / Bhat, Sinchana G / Ghate, Sudeep D / Rao, R Shyama Prasad / Kumar, R Ajay / Kurthkoti, Krishna

    Microbial pathogenesis

    2023  Volume 185, Page(s) 106384

    Abstract: Mycobacterium tuberculosis is a leading cause of human mortality worldwide, and the emergence of drug-resistant strains demands the discovery of new classes of antimycobacterial that can be employed in the therapeutic pipeline. Previously, a secondary ... ...

    Abstract Mycobacterium tuberculosis is a leading cause of human mortality worldwide, and the emergence of drug-resistant strains demands the discovery of new classes of antimycobacterial that can be employed in the therapeutic pipeline. Previously, a secondary metabolite, chrysomycin A, isolated from Streptomyces sp. OA161 displayed potent bactericidal activity against drug-resistant clinical isolates of M. tuberculosis and different species of mycobacteria. The antibiotic inhibits mycobacterial topoisomerase I and DNA gyrase, leading to bacterial death, but the mechanisms that could cause resistance to this antibiotic are currently unknown. To further understand the resistance mechanism, using M. smegmatis as a model, spontaneous resistance mutants were isolated and subjected to whole-genome sequencing. Mutation in a Tet
    MeSH term(s) Humans ; Mycobacterium smegmatis/genetics ; Mycobacterium smegmatis/metabolism ; Anti-Bacterial Agents/pharmacology ; Anti-Bacterial Agents/metabolism ; Mycobacterium tuberculosis/genetics ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Drug Resistance, Multiple, Bacterial/genetics ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism
    Chemical Substances Anti-Bacterial Agents ; Membrane Transport Proteins ; Bacterial Proteins
    Language English
    Publishing date 2023-10-12
    Publishing country England
    Document type Journal Article
    ZDB-ID 632772-2
    ISSN 1096-1208 ; 0882-4010
    ISSN (online) 1096-1208
    ISSN 0882-4010
    DOI 10.1016/j.micpath.2023.106384
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2136: Show issues Location:
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  3. Article ; Online: Chrysomycin A inhibits the topoisomerase I of Mycobacterium tuberculosis.

    Muralikrishnan, Balaji / Edison, Lekshmi K / Dusthackeer, Azger / Jijimole, G R / Ramachandran, Ranjit / Madhavan, Aravind / Kumar, Ramakrishnan Ajay

    The Journal of antibiotics

    2022  Volume 75, Issue 4, Page(s) 226–235

    Abstract: Novel anti-tuberculosis drugs are essential to manage drug-resistant tuberculosis, caused by Mycobacterium tuberculosis. We recently reported the antimycobacterial activity of chrysomycin A in vitro and in infected macrophages. In this study, we report ... ...

    Abstract Novel anti-tuberculosis drugs are essential to manage drug-resistant tuberculosis, caused by Mycobacterium tuberculosis. We recently reported the antimycobacterial activity of chrysomycin A in vitro and in infected macrophages. In this study, we report that it inhibits the growth of drug-resistant clinical strains of M. tuberculosis and acts in synergy with anti-TB drugs such as ethambutol, ciprofloxacin, and novobiocin. In pursuit of its mechanism of action, it was found that chrysomycin A is bactericidal and exerts this activity by interacting with DNA at specific sequences and by inhibiting the topoisomerase I activity of M. tuberculosis. It also exhibits weak inhibition of the DNA gyrase enzyme of the pathogen.
    MeSH term(s) Aminoglycosides ; Antitubercular Agents/pharmacology ; DNA Topoisomerases, Type I ; Humans ; Microbial Sensitivity Tests ; Mycobacterium tuberculosis ; Tuberculosis
    Chemical Substances Aminoglycosides ; Antitubercular Agents ; chrysomycin A (82196-88-1) ; DNA Topoisomerases, Type I (EC 5.99.1.2)
    Language English
    Publishing date 2022-02-08
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 390800-8
    ISSN 1881-1469 ; 0021-8820 ; 0368-3532
    ISSN (online) 1881-1469
    ISSN 0021-8820 ; 0368-3532
    DOI 10.1038/s41429-022-00503-z
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 207: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  4. Article: Anti-microbial activity of chrysomycin A produced by Streptomyces sp. against Mycobacterium tuberculosis

    Muralikrishnan, Balaji / Dan, Vipin Mohan / Vinodh, J. S / Jamsheena, Vellekkatt / Ramachandran, Ranjit / Thomas, Sabu / Dastager, Syed G / Kumar, K. Santhosh / Lankalapalli, Ravi Shankar / Kumar, Ramakrishnan Ajay

    RSC advances. 2017 July 21, v. 7, no. 58

    2017  

    Abstract: Limited efficacy of the BCG (Bacillus Calmette–Guérin) vaccine against adult tuberculosis and the emergence of resistance to existing anti-tuberculosis drugs compel discovery of novel antibiotics against Mycobacterium tuberculosis. Actinomycetes are ... ...

    Abstract Limited efficacy of the BCG (Bacillus Calmette–Guérin) vaccine against adult tuberculosis and the emergence of resistance to existing anti-tuberculosis drugs compel discovery of novel antibiotics against Mycobacterium tuberculosis. Actinomycetes are still an attractive platform for the discovery of new antimicrobials, especially from untapped natural hotspots, despite the belief that they are an exhausted resource after repeated re-discoveries. Herein we report the isolation and identification of chrysomycin A from an actinomycete isolated from a coastal area in Kerala. We show for the first time that it has antimycobacterial activity. It was found to be bactericidal to planktonic and intracellular M. tuberculosis with an MIC of 3.125 μg mL−1; it is non-hemolytic and has negligible cytotoxicity. The actinomycete that produces chrysomycin A was found to be a Streptomyces sp. through 16S rRNA gene sequencing.
    Keywords Mycobacterium bovis BCG ; Mycobacterium tuberculosis ; Streptomyces ; adults ; antibacterial properties ; antibiotics ; coasts ; cytotoxicity ; plankton ; ribosomal RNA ; sequence analysis ; tuberculosis ; vaccines ; India
    Language English
    Dates of publication 2017-0721
    Size p. 36335-36339.
    Publishing place The Royal Society of Chemistry
    Document type Article
    ISSN 2046-2069
    DOI 10.1039/c7ra05576e
    Database NAL-Catalogue (AGRICOLA)

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  5. Article ; Online: The multiple stress responsive transcriptional regulator Rv3334 of Mycobacterium tuberculosis is an autorepressor and a positive regulator of kstR.

    Gomez, Roshna Lawrence / Jose, Leny / Ramachandran, Ranjit / Raghunandanan, Sajith / Muralikrishnan, Balaji / Johnson, John Bernet / Sivakumar, Krishnankutty Chandrika / Mundayoor, Sathish / Kumar, Ramakrishnan Ajay

    The FEBS journal

    2016  Volume 283, Issue 16, Page(s) 3056–3071

    Abstract: Rv3334 protein of Mycobacterium tuberculosis belongs to the MerR family of transcriptional regulators and is upregulated during hypoxia and other stress conditions. Employing GFP reporter constructs, mobility shift assays and ChIP assays, we demonstrate ... ...

    Abstract Rv3334 protein of Mycobacterium tuberculosis belongs to the MerR family of transcriptional regulators and is upregulated during hypoxia and other stress conditions. Employing GFP reporter constructs, mobility shift assays and ChIP assays, we demonstrate that Rv3334 binds to its own promoter and acts as an autorepressor. We were able to locate a 22 bp palindrome in its promoter that we show to be the cognate binding sequence of Rv3334. Using chase experiments, we could conclusively prove the requirement of this palindrome for Rv3334 binding. Recombinant Rv3334 readily formed homodimers in vitro, which could be necessary for its transcriptional regulatory role in vivo. Although the DNA-binding activity of the protein was abrogated by the presence of certain divalent metal cations, the homodimer formation remained unaffected. In silico predictions and subsequent assays using GFP reporter constructs and mobility shift assays revealed that the expression of ketosteroid regulator gene (kstR), involved in lipid catabolism, is positively regulated by Rv3334. ChIP assays with aerobically grown M. tuberculosis as well as dormant bacteria unambiguously prove that Rv3334 specifically upregulates expression of kstR during dormancy. Our study throws light on the possible role of Rv3334 as a master regulator of lipid catabolism during hypoxia-induced dormancy.
    MeSH term(s) Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; DNA/metabolism ; Gene Expression Regulation, Bacterial ; Inverted Repeat Sequences ; Metals, Heavy/metabolism ; Mycobacterium tuberculosis/genetics ; Mycobacterium tuberculosis/metabolism ; Promoter Regions, Genetic ; Protein Binding ; Protein Multimerization ; Repressor Proteins/metabolism ; Up-Regulation
    Chemical Substances Bacterial Proteins ; Metals, Heavy ; Repressor Proteins ; DNA (9007-49-2)
    Language English
    Publishing date 2016-08
    Publishing country England
    Document type Journal Article
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.13791
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 260: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  6. Article ; Online: Streptomyces sp metabolite(s) promotes Bax mediated intrinsic apoptosis and autophagy involving inhibition of mTOR pathway in cervical cancer cell lines.

    Dan, Vipin Mohan / Muralikrishnan, Balaji / Sanawar, Rahul / J S, Vinodh / Burkul, Bhushan Bapusaheb / Srinivas, Kalanghad Puthankalam / Lekshmi, Asha / Pradeep, N S / Dastager, Syed G / Santhakumari, B / Santhoshkumar, Thankayyan R / Kumar, R Ajay / Pillai, Madhavan Radhakrishna

    Scientific reports

    2018  Volume 8, Issue 1, Page(s) 2810

    Abstract: In cervical cancer, the association between HPV infection and dysregulation of phosphoinositide 3-kinase (PI3K)/protein kinase B (AKT)/mammalian target of rapamycin (mTOR) pathway (PI3K/AKT/mTOR pathway) places mTOR as an attractive therapeutic target. ... ...

    Abstract In cervical cancer, the association between HPV infection and dysregulation of phosphoinositide 3-kinase (PI3K)/protein kinase B (AKT)/mammalian target of rapamycin (mTOR) pathway (PI3K/AKT/mTOR pathway) places mTOR as an attractive therapeutic target. The failure of current treatment modalities in advanced stages of this cancer and drawbacks of already available mTOR inhibitors demand for novel drug candidates. In the present study we identified the presence of a mTOR inhibitor in an active fraction of the ethyl acetate extract of Streptomyces sp OA293. The metabolites(s) in the active fraction completely inhibited mTORC1 and thereby suppressed activation of both of its downstream targets, 4E-BP1 and P70S6k, in cervical cancer cells. In addition, it also stalled Akt activation via inhibition of mTORC2. The mechanism of mTOR inhibition detailed in our study overcomes significant drawbacks of well known mTOR inhibitors such as rapamycin and rapalogs. The active fraction induced autophagy and Bax mediated apoptosis suggesting that mTOR inhibition resulted in programmed cell death of cancer cells. The molecular weight determination of the components in active fraction confirmed the absence of any previously known natural mTOR inhibitor. This is the first report of complete mTOR complex inhibition by a product derived from microbial source.
    MeSH term(s) Apoptosis/drug effects ; Apoptosis/physiology ; Autophagy/drug effects ; Autophagy/physiology ; Biological Products/pharmacology ; Cell Line, Tumor ; Cell Proliferation/drug effects ; Female ; HEK293 Cells ; Humans ; Mechanistic Target of Rapamycin Complex 1/metabolism ; Phosphatidylinositol 3-Kinase/metabolism ; Phosphatidylinositol 3-Kinases/metabolism ; Protein Kinase Inhibitors/pharmacology ; Proto-Oncogene Proteins c-akt/metabolism ; Signal Transduction/drug effects ; Sirolimus/pharmacology ; Streptomyces/chemistry ; Streptomyces/metabolism ; TOR Serine-Threonine Kinases/antagonists & inhibitors ; TOR Serine-Threonine Kinases/metabolism ; Uterine Cervical Neoplasms/metabolism ; bcl-2-Associated X Protein/metabolism
    Chemical Substances BAX protein, human ; Biological Products ; Protein Kinase Inhibitors ; bcl-2-Associated X Protein ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; MTOR protein, human (EC 2.7.1.1) ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; Phosphatidylinositol 3-Kinase (EC 2.7.1.137) ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; Sirolimus (W36ZG6FT64)
    Language English
    Publishing date 2018-02-12
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-018-21249-5
    Database MEDical Literature Analysis and Retrieval System OnLINE

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