Improved production of A40926 by Nonomuraea sp. through deletion of a pathway-specific acetyltransferase
Nonomuraea strain ATCC 39727 produces the glycopeptide A40926, used for manufacturing dalbavancin, currently in advanced clinical trials. From the gene cluster involved in A40926 biosynthesis, a strain deleted in dbv23 was constructed. This mutant can produce only the glycopeptides lacking the O-lin...
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| Veröffentlicht in: | Applied microbiology and biotechnology 2010-08, Vol.87 (5), p.1633-1638 |
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| creator | Sosio, Margherita Canavesi, Augusto Stinchi, Sofia Donadio, Stefano |
| description | Nonomuraea strain ATCC 39727 produces the glycopeptide A40926, used for manufacturing dalbavancin, currently in advanced clinical trials. From the gene cluster involved in A40926 biosynthesis, a strain deleted in dbv23 was constructed. This mutant can produce only the glycopeptides lacking the O-linked acetyl residue at position 6 of the mannose moiety, while, under identical fermentation conditions, the wild-type strain produces mostly glycopeptides carrying an acetylated mannose. Furthermore, the total amount of glycopeptides produced by the mutant strain was found to be approximately twice that of the wild type. The reduced level of glycopeptides observed in the wild-type strain may be due to an inhibitory effect exerted by the acetylated compound on the biosynthesis of A40926. Indeed, spiking production cultures with ≥1 μg/ml of the acetylated glycopeptide inhibited A40926 production in the mutant strain. |
| doi_str_mv | 10.1007/s00253-010-2579-2 |
| format | Article |
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From the gene cluster involved in A40926 biosynthesis, a strain deleted in dbv23 was constructed. This mutant can produce only the glycopeptides lacking the O-linked acetyl residue at position 6 of the mannose moiety, while, under identical fermentation conditions, the wild-type strain produces mostly glycopeptides carrying an acetylated mannose. Furthermore, the total amount of glycopeptides produced by the mutant strain was found to be approximately twice that of the wild type. The reduced level of glycopeptides observed in the wild-type strain may be due to an inhibitory effect exerted by the acetylated compound on the biosynthesis of A40926. Indeed, spiking production cultures with ≥1 μg/ml of the acetylated glycopeptide inhibited A40926 production in the mutant strain.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-010-2579-2</identifier><identifier>PMID: 20414653</identifier><identifier>CODEN: AMBIDG</identifier><language>eng</language><publisher>Berlin/Heidelberg: Berlin/Heidelberg : Springer-Verlag</publisher><subject>Acetyltransferase ; Acetyltransferases - genetics ; Actinomycetales ; Actinomycetales - enzymology ; Actinomycetales - genetics ; Actinomycetales - metabolism ; Anti-Bacterial Agents - biosynthesis ; Antibiotics ; Antimicrobial agents ; Bacterial Proteins - genetics ; Biological and medical sciences ; Biomedical and Life Sciences ; Biosynthesis ; Biotechnological Products and Process Engineering ; Biotechnology ; Chromatography, High Pressure Liquid ; Fermentation ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation, Enzymologic ; glycopeptides ; Life Sciences ; Metabolites ; Microbial Genetics and Genomics ; Microbiology ; Molecular Structure ; Multigene Family ; Sequence Deletion ; Sodium ; Studies ; Teicoplanin - analogs & derivatives ; Teicoplanin - biosynthesis</subject><ispartof>Applied microbiology and biotechnology, 2010-08, Vol.87 (5), p.1633-1638</ispartof><rights>Springer-Verlag 2010</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c456t-3408b7dde4329e4733fa5f1477e34c10996618001aa39e77061622e85765c19f3</citedby><cites>FETCH-LOGICAL-c456t-3408b7dde4329e4733fa5f1477e34c10996618001aa39e77061622e85765c19f3</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/s00253-010-2579-2$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00253-010-2579-2$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51298</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23049988$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20414653$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sosio, Margherita</creatorcontrib><creatorcontrib>Canavesi, Augusto</creatorcontrib><creatorcontrib>Stinchi, Sofia</creatorcontrib><creatorcontrib>Donadio, Stefano</creatorcontrib><title>Improved production of A40926 by Nonomuraea sp. through deletion of a pathway-specific acetyltransferase</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>Nonomuraea strain ATCC 39727 produces the glycopeptide A40926, used for manufacturing dalbavancin, currently in advanced clinical trials. From the gene cluster involved in A40926 biosynthesis, a strain deleted in dbv23 was constructed. This mutant can produce only the glycopeptides lacking the O-linked acetyl residue at position 6 of the mannose moiety, while, under identical fermentation conditions, the wild-type strain produces mostly glycopeptides carrying an acetylated mannose. Furthermore, the total amount of glycopeptides produced by the mutant strain was found to be approximately twice that of the wild type. The reduced level of glycopeptides observed in the wild-type strain may be due to an inhibitory effect exerted by the acetylated compound on the biosynthesis of A40926. Indeed, spiking production cultures with ≥1 μg/ml of the acetylated glycopeptide inhibited A40926 production in the mutant strain.</description><subject>Acetyltransferase</subject><subject>Acetyltransferases - genetics</subject><subject>Actinomycetales</subject><subject>Actinomycetales - enzymology</subject><subject>Actinomycetales - genetics</subject><subject>Actinomycetales - metabolism</subject><subject>Anti-Bacterial Agents - biosynthesis</subject><subject>Antibiotics</subject><subject>Antimicrobial agents</subject><subject>Bacterial Proteins - genetics</subject><subject>Biological and medical sciences</subject><subject>Biomedical and Life Sciences</subject><subject>Biosynthesis</subject><subject>Biotechnological Products and Process Engineering</subject><subject>Biotechnology</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Fermentation</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>glycopeptides</subject><subject>Life Sciences</subject><subject>Metabolites</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>Molecular Structure</subject><subject>Multigene Family</subject><subject>Sequence Deletion</subject><subject>Sodium</subject><subject>Studies</subject><subject>Teicoplanin - analogs & derivatives</subject><subject>Teicoplanin - biosynthesis</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqFks1u1DAUhS1ERYfCA7ABCwmxSvG_42VVFahUtYvSteVxrmdSJXGwk6J5-3rIlEosYHUX_s65Pj5G6B0lp5QQ_SUTwiSvCCUVk9pU7AVaUcFZRRQVL9GKUC0rLU19jF7nfE8IZbVSr9AxI4IKJfkKbS_7McUHaHAZzeynNg44BnwmiGEKr3f4Og6xn5MDh_N4iqdtivNmixvo4Al2eHTT9pfbVXkE34bWY-dh2nVTckMOkFyGN-gouC7D28M8QXdfL36cf6-ubr5dnp9dVV5INVVckHqtmwZKDANCcx6cDFRoDVx4SoxRitYliXPcgNYlqWIMaqmV9NQEfoI-L74lz88Z8mT7NnvoOjdAnLPVUtS1oLX-P8m50UazPfnxL_I-zmkoMayiXCtRLAtEF8inmHOCYMfU9i7tLCV2X5dd6rKlLruvy7KieX8wntc9NH8UT_0U4NMBcNm7LpT39G1-5jgRxvxezhYul6NhA-n5hv_a_mERBRet26RifHfLCOWE1kqXn8IfAZD7s3w</recordid><startdate>20100801</startdate><enddate>20100801</enddate><creator>Sosio, Margherita</creator><creator>Canavesi, Augusto</creator><creator>Stinchi, Sofia</creator><creator>Donadio, Stefano</creator><general>Berlin/Heidelberg : Springer-Verlag</general><general>Springer-Verlag</general><general>Springer</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>IQODW</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>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>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>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>M2P</scope><scope>M7N</scope><scope>M7P</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>20100801</creationdate><title>Improved production of A40926 by Nonomuraea sp. through deletion of a pathway-specific acetyltransferase</title><author>Sosio, Margherita ; Canavesi, Augusto ; Stinchi, Sofia ; Donadio, Stefano</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c456t-3408b7dde4329e4733fa5f1477e34c10996618001aa39e77061622e85765c19f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Acetyltransferase</topic><topic>Acetyltransferases - genetics</topic><topic>Actinomycetales</topic><topic>Actinomycetales - enzymology</topic><topic>Actinomycetales - genetics</topic><topic>Actinomycetales - metabolism</topic><topic>Anti-Bacterial Agents - biosynthesis</topic><topic>Antibiotics</topic><topic>Antimicrobial agents</topic><topic>Bacterial Proteins - genetics</topic><topic>Biological and medical sciences</topic><topic>Biomedical and Life Sciences</topic><topic>Biosynthesis</topic><topic>Biotechnological Products and Process Engineering</topic><topic>Biotechnology</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Fermentation</topic><topic>Fundamental and applied biological sciences. 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From the gene cluster involved in A40926 biosynthesis, a strain deleted in dbv23 was constructed. This mutant can produce only the glycopeptides lacking the O-linked acetyl residue at position 6 of the mannose moiety, while, under identical fermentation conditions, the wild-type strain produces mostly glycopeptides carrying an acetylated mannose. Furthermore, the total amount of glycopeptides produced by the mutant strain was found to be approximately twice that of the wild type. The reduced level of glycopeptides observed in the wild-type strain may be due to an inhibitory effect exerted by the acetylated compound on the biosynthesis of A40926. Indeed, spiking production cultures with ≥1 μg/ml of the acetylated glycopeptide inhibited A40926 production in the mutant strain.</abstract><cop>Berlin/Heidelberg</cop><pub>Berlin/Heidelberg : Springer-Verlag</pub><pmid>20414653</pmid><doi>10.1007/s00253-010-2579-2</doi><tpages>6</tpages></addata></record> |
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| subjects | Acetyltransferase Acetyltransferases - genetics Actinomycetales Actinomycetales - enzymology Actinomycetales - genetics Actinomycetales - metabolism Anti-Bacterial Agents - biosynthesis Antibiotics Antimicrobial agents Bacterial Proteins - genetics Biological and medical sciences Biomedical and Life Sciences Biosynthesis Biotechnological Products and Process Engineering Biotechnology Chromatography, High Pressure Liquid Fermentation Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Enzymologic glycopeptides Life Sciences Metabolites Microbial Genetics and Genomics Microbiology Molecular Structure Multigene Family Sequence Deletion Sodium Studies Teicoplanin - analogs & derivatives Teicoplanin - biosynthesis |
| title | Improved production of A40926 by Nonomuraea sp. through deletion of a pathway-specific acetyltransferase |
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