Anti-tuberculosis lead molecules from natural products targeting Mycobacterium tuberculosis ClpC1
Tuberculosis (TB) is a serious and potentially fatal disease caused by Mycobacterium tuberculosis (M. tb). The occurrence of multidrug-resistant (MDR) and extensively drug-resistant (XDR) M. tb is a significant public health concern because most of the anti-TB drugs that have been in use for over 40...
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description | Tuberculosis (TB) is a serious and potentially fatal disease caused by Mycobacterium tuberculosis (M. tb). The occurrence of multidrug-resistant (MDR) and extensively drug-resistant (XDR) M. tb is a significant public health concern because most of the anti-TB drugs that have been in use for over 40 years are no longer effective for the treatment of these infections. Recently, new anti-TB lead compounds such as cyclomarin A, lassomycin, and ecumicin, which are cyclic peptides from actinomycetes, have shown potent anti-TB activity against MDR and XDR M. tb as well as drug-susceptible M. tb in vitro. The target molecule of these antibiotics is ClpC1, a protein that is essential for the growth of M. tb. In this review, we introduce the three anti-TB lead compounds as potential anti-TB therapeutic agents targeting ClpC1 and compare them with the existing anti-TB drugs approved by the US Food and Drug Administration. |
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The occurrence of multidrug-resistant (MDR) and extensively drug-resistant (XDR) M. tb is a significant public health concern because most of the anti-TB drugs that have been in use for over 40 years are no longer effective for the treatment of these infections. Recently, new anti-TB lead compounds such as cyclomarin A, lassomycin, and ecumicin, which are cyclic peptides from actinomycetes, have shown potent anti-TB activity against MDR and XDR M. tb as well as drug-susceptible M. tb in vitro. The target molecule of these antibiotics is ClpC1, a protein that is essential for the growth of M. tb. In this review, we introduce the three anti-TB lead compounds as potential anti-TB therapeutic agents targeting ClpC1 and compare them with the existing anti-TB drugs approved by the US Food and Drug Administration.</description><identifier>ISSN: 1367-5435</identifier><identifier>EISSN: 1476-5535</identifier><identifier>DOI: 10.1007/s10295-015-1709-3</identifier><identifier>PMID: 26586403</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Antibiotics ; Antitubercular Agents - isolation & purification ; Antitubercular Agents - pharmacology ; Bacteria ; Biochemistry ; Bioinformatics ; Biological Products - chemistry ; Biomedical and Life Sciences ; Biomedical research ; Biotechnology ; cyclic peptides ; Dihydrofolate reductase ; Drug Approval ; Drug resistance ; drugs ; Extensively Drug-Resistant Tuberculosis - drug therapy ; Extensively Drug-Resistant Tuberculosis - microbiology ; FDA approval ; Genetic Engineering ; HIV ; Human immunodeficiency virus ; Humans ; Infections ; Infectious diseases ; Inorganic Chemistry ; Life Sciences ; Microbiology ; Mini-Review ; multiple drug resistance ; Mycobacterium tuberculosis ; Mycobacterium tuberculosis - classification ; Mycobacterium tuberculosis - drug effects ; Natural products ; Peptides ; Peptides, Cyclic - isolation & purification ; Peptides, Cyclic - pharmacology ; Proteins ; Public health ; RNA polymerase ; Studies ; Tuberculosis ; Tuberculosis, Multidrug-Resistant - drug therapy ; Tuberculosis, Multidrug-Resistant - microbiology ; United States ; United States Food and Drug Administration</subject><ispartof>Journal of industrial microbiology & biotechnology, 2016-03, Vol.43 (2-3), p.205-212</ispartof><rights>Society for Industrial Microbiology 2016 2016</rights><rights>Society for Industrial Microbiology and Biotechnology 2015</rights><rights>Society for Industrial Microbiology and Biotechnology 2016</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c503t-d7335845934ac2ae4206c0e8965e3dc1a138c1d4c2f9e60381b6a1b4b096fe623</citedby><cites>FETCH-LOGICAL-c503t-d7335845934ac2ae4206c0e8965e3dc1a138c1d4c2f9e60381b6a1b4b096fe623</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10295-015-1709-3$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10295-015-1709-3$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>313,314,776,780,788,27899,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26586403$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lee, Hanki</creatorcontrib><creatorcontrib>Suh, Joo-Won</creatorcontrib><title>Anti-tuberculosis lead molecules from natural products targeting Mycobacterium tuberculosis ClpC1</title><title>Journal of industrial microbiology & biotechnology</title><addtitle>J Ind Microbiol Biotechnol</addtitle><addtitle>J Ind Microbiol Biotechnol</addtitle><description>Tuberculosis (TB) is a serious and potentially fatal disease caused by Mycobacterium tuberculosis (M. tb). The occurrence of multidrug-resistant (MDR) and extensively drug-resistant (XDR) M. tb is a significant public health concern because most of the anti-TB drugs that have been in use for over 40 years are no longer effective for the treatment of these infections. Recently, new anti-TB lead compounds such as cyclomarin A, lassomycin, and ecumicin, which are cyclic peptides from actinomycetes, have shown potent anti-TB activity against MDR and XDR M. tb as well as drug-susceptible M. tb in vitro. The target molecule of these antibiotics is ClpC1, a protein that is essential for the growth of M. tb. In this review, we introduce the three anti-TB lead compounds as potential anti-TB therapeutic agents targeting ClpC1 and compare them with the existing anti-TB drugs approved by the US Food and Drug Administration.</description><subject>Antibiotics</subject><subject>Antitubercular Agents - isolation & purification</subject><subject>Antitubercular Agents - pharmacology</subject><subject>Bacteria</subject><subject>Biochemistry</subject><subject>Bioinformatics</subject><subject>Biological Products - chemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedical research</subject><subject>Biotechnology</subject><subject>cyclic peptides</subject><subject>Dihydrofolate reductase</subject><subject>Drug Approval</subject><subject>Drug resistance</subject><subject>drugs</subject><subject>Extensively Drug-Resistant Tuberculosis - drug therapy</subject><subject>Extensively Drug-Resistant Tuberculosis - microbiology</subject><subject>FDA approval</subject><subject>Genetic Engineering</subject><subject>HIV</subject><subject>Human immunodeficiency virus</subject><subject>Humans</subject><subject>Infections</subject><subject>Infectious diseases</subject><subject>Inorganic Chemistry</subject><subject>Life Sciences</subject><subject>Microbiology</subject><subject>Mini-Review</subject><subject>multiple drug resistance</subject><subject>Mycobacterium tuberculosis</subject><subject>Mycobacterium tuberculosis - classification</subject><subject>Mycobacterium tuberculosis - drug effects</subject><subject>Natural products</subject><subject>Peptides</subject><subject>Peptides, Cyclic - isolation & purification</subject><subject>Peptides, Cyclic - pharmacology</subject><subject>Proteins</subject><subject>Public health</subject><subject>RNA polymerase</subject><subject>Studies</subject><subject>Tuberculosis</subject><subject>Tuberculosis, Multidrug-Resistant - drug therapy</subject><subject>Tuberculosis, Multidrug-Resistant - microbiology</subject><subject>United States</subject><subject>United States Food and Drug Administration</subject><issn>1367-5435</issn><issn>1476-5535</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqNkktv1TAQhS0EouXCD2ADkdiwwDDjZ7KsrnhJRSyga8txnKtUSXzxY9F_X1-loIIEYmXL_s6ZGR8T8hzhLQLodwmBdZICSooaOsofkHMUWlEpuXxY91xpKgWXZ-RJStcAILVmj8kZU7JVAvg5sRdrnmguvY-uzCFNqZm9HZolzL4e-NSMMSzNanOJdm6OMQzF5dRkGw8-T-uh-XLjQm9d9nEqS_Ob034-7vEpeTTaOflnd-uOXH14_33_iV5-_fh5f3FJnQSe6aA5l62QHRfWMesFA-XAt52Sng8OLfLW4SAcGzuvgLfYK4u96KFTo1eM78jrzbf2-KP4lM0yJefn2a4-lGRQq7aOrxH_B5WIQtQX2pFXf6DXocS1DnKiRMu5QF4p3CgXQ0rRj-YYp8XGG4NgTlGZLSpTozKnqMxJ8-LOufSLH34pfmZTAbYBqV6tBx_vlf6H65tNFMrxL03c-y8Vf7nhow3GHuKUzNU3BqgAEEF0yG8BoS6z2A</recordid><startdate>20160301</startdate><enddate>20160301</enddate><creator>Lee, Hanki</creator><creator>Suh, Joo-Won</creator><general>Springer Berlin Heidelberg</general><general>Oxford University Press</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7QR</scope><scope>7T7</scope><scope>7WY</scope><scope>7WZ</scope><scope>7X7</scope><scope>7XB</scope><scope>87Z</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8FL</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BEZIV</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FRNLG</scope><scope>FYUFA</scope><scope>F~G</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K60</scope><scope>K6~</scope><scope>K9.</scope><scope>L.-</scope><scope>LK8</scope><scope>M0C</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQBIZ</scope><scope>PQBZA</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>7QO</scope></search><sort><creationdate>20160301</creationdate><title>Anti-tuberculosis lead molecules from natural products targeting Mycobacterium tuberculosis ClpC1</title><author>Lee, Hanki ; Suh, Joo-Won</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c503t-d7335845934ac2ae4206c0e8965e3dc1a138c1d4c2f9e60381b6a1b4b096fe623</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Antibiotics</topic><topic>Antitubercular Agents - 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The occurrence of multidrug-resistant (MDR) and extensively drug-resistant (XDR) M. tb is a significant public health concern because most of the anti-TB drugs that have been in use for over 40 years are no longer effective for the treatment of these infections. Recently, new anti-TB lead compounds such as cyclomarin A, lassomycin, and ecumicin, which are cyclic peptides from actinomycetes, have shown potent anti-TB activity against MDR and XDR M. tb as well as drug-susceptible M. tb in vitro. The target molecule of these antibiotics is ClpC1, a protein that is essential for the growth of M. tb. In this review, we introduce the three anti-TB lead compounds as potential anti-TB therapeutic agents targeting ClpC1 and compare them with the existing anti-TB drugs approved by the US Food and Drug Administration.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>26586403</pmid><doi>10.1007/s10295-015-1709-3</doi><tpages>8</tpages></addata></record> |
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subjects | Antibiotics Antitubercular Agents - isolation & purification Antitubercular Agents - pharmacology Bacteria Biochemistry Bioinformatics Biological Products - chemistry Biomedical and Life Sciences Biomedical research Biotechnology cyclic peptides Dihydrofolate reductase Drug Approval Drug resistance drugs Extensively Drug-Resistant Tuberculosis - drug therapy Extensively Drug-Resistant Tuberculosis - microbiology FDA approval Genetic Engineering HIV Human immunodeficiency virus Humans Infections Infectious diseases Inorganic Chemistry Life Sciences Microbiology Mini-Review multiple drug resistance Mycobacterium tuberculosis Mycobacterium tuberculosis - classification Mycobacterium tuberculosis - drug effects Natural products Peptides Peptides, Cyclic - isolation & purification Peptides, Cyclic - pharmacology Proteins Public health RNA polymerase Studies Tuberculosis Tuberculosis, Multidrug-Resistant - drug therapy Tuberculosis, Multidrug-Resistant - microbiology United States United States Food and Drug Administration |
title | Anti-tuberculosis lead molecules from natural products targeting Mycobacterium tuberculosis ClpC1 |
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