Multiple FadD acyl-CoA synthetases contribute to differential fatty acid degradation and virulence in Pseudomonas aeruginosa
A close interconnection between nutrient metabolism and virulence factor expression contributes to the pathophysiology of Pseudomonas aeruginosa as a successful pathogen. P. aeruginosa fatty acid (FA) degradation is complicated with multiple acyl-CoA synthetase homologs (FadDs) expressed in vivo in...
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| description | A close interconnection between nutrient metabolism and virulence factor expression contributes to the pathophysiology of Pseudomonas aeruginosa as a successful pathogen. P. aeruginosa fatty acid (FA) degradation is complicated with multiple acyl-CoA synthetase homologs (FadDs) expressed in vivo in lung tissue during cystic fibrosis infections. The promoters of two genetically linked P. aeruginosa fadD genes (fadD1 and fadD2) were mapped and northern blot analysis indicated they could exist on two different transcripts. These FadDs contain ATP/AMP signature and FA-binding motifs highly homologous to those of the Escherichia coli FadD. Upon introduction into an E. coli fadD(-)/fadR(-) double mutant, both P. aeruginosa fadDs functionally complemented the E. coli fadD(-)/fadR(-) mutant, allowing degradation of different chain-length FAs. Chromosomal mutagenesis, growth analysis, induction studies, and determination of kinetic parameters suggested that FadD1 has a substrate preference for long-chain FAs while FadD2 prefers shorter-chain FAs. When compared to the wild type strain, the fadD2 mutant exhibited decreased production of lipase, protease, rhamnolipid and phospholipase, and retardation of both swimming and swarming motilities. Interestingly, fadD1 mutant showed only increased swarming motility. Growth analysis of the fadD mutants showed noticeable deficiencies in utilizing FAs and phosphatidylcholine (major components of lung surfactant) as the sole carbon source. This defect translated into decreased in vivo fitness of P. aeruginosa in a BALB/c mouse lung infection model, supporting the role of lipids as a significant nutrient source for this bacterium in vivo. |
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P. aeruginosa fatty acid (FA) degradation is complicated with multiple acyl-CoA synthetase homologs (FadDs) expressed in vivo in lung tissue during cystic fibrosis infections. The promoters of two genetically linked P. aeruginosa fadD genes (fadD1 and fadD2) were mapped and northern blot analysis indicated they could exist on two different transcripts. These FadDs contain ATP/AMP signature and FA-binding motifs highly homologous to those of the Escherichia coli FadD. Upon introduction into an E. coli fadD(-)/fadR(-) double mutant, both P. aeruginosa fadDs functionally complemented the E. coli fadD(-)/fadR(-) mutant, allowing degradation of different chain-length FAs. Chromosomal mutagenesis, growth analysis, induction studies, and determination of kinetic parameters suggested that FadD1 has a substrate preference for long-chain FAs while FadD2 prefers shorter-chain FAs. When compared to the wild type strain, the fadD2 mutant exhibited decreased production of lipase, protease, rhamnolipid and phospholipase, and retardation of both swimming and swarming motilities. Interestingly, fadD1 mutant showed only increased swarming motility. Growth analysis of the fadD mutants showed noticeable deficiencies in utilizing FAs and phosphatidylcholine (major components of lung surfactant) as the sole carbon source. This defect translated into decreased in vivo fitness of P. aeruginosa in a BALB/c mouse lung infection model, supporting the role of lipids as a significant nutrient source for this bacterium in vivo.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0013557</identifier><identifier>PMID: 21042406</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino Acid Sequence ; AMP ; Analysis ; Base Sequence ; Biodegradation ; Bioengineering ; Biosynthesis ; Carbon sources ; Chains ; Cloning ; Coenzyme A Ligases - chemistry ; Coenzyme A Ligases - genetics ; Coenzyme A Ligases - metabolism ; Cystic fibrosis ; Degradation ; Dehydrogenases ; DNA, Bacterial ; E coli ; Enzymes ; Escherichia coli ; Escherichia coli - enzymology ; FADD protein ; Fatty acids ; Fatty Acids - metabolism ; Fitness ; Genes ; Genetic aspects ; Genetics and Genomics/Gene Expression ; Genetics and Genomics/Gene Function ; Genomes ; Health aspects ; Homology ; Hydrolysis ; Infections ; Infectious Diseases/Bacterial Infections ; Infectious Diseases/Respiratory Infections ; Kinetics ; Lecithin ; Ligases ; Lipase ; Lipids ; Lungs ; Metabolism ; Microbiology/Microbial Physiology and Metabolism ; Molecular Sequence Data ; Motility ; Mutagenesis ; Mutants ; Mutation ; Nutrients ; Phosphatidylcholine ; Phospholipase ; Phospholipids ; Physical fitness ; Physiological aspects ; Plant engineering ; Proteases ; Proteins ; Pseudomonas ; Pseudomonas aeruginosa ; Pseudomonas aeruginosa - enzymology ; Pseudomonas aeruginosa - pathogenicity ; RNA, Messenger - genetics ; Sequence Homology, Amino Acid ; Substrate Specificity ; Surfactants ; Swarming ; Swimming ; Tuberculosis ; Vectors (Biology) ; Virulence ; Virulence (Microbiology) ; Virulence factors</subject><ispartof>PloS one, 2010-10, Vol.5 (10), p.e13557</ispartof><rights>COPYRIGHT 2010 Public Library of Science</rights><rights>2010 Kang et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Kang et al. 2010</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c723t-806e38baab6b54f5447485d7a0bb9a28f50104691d0b64db720bf950ff527e383</citedby><cites>FETCH-LOGICAL-c723t-806e38baab6b54f5447485d7a0bb9a28f50104691d0b64db720bf950ff527e383</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2958839/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2958839/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79343,79344</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21042406$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kang, Yun</creatorcontrib><creatorcontrib>Zarzycki-Siek, Jan</creatorcontrib><creatorcontrib>Walton, Chad B</creatorcontrib><creatorcontrib>Norris, Michael H</creatorcontrib><creatorcontrib>Hoang, Tung T</creatorcontrib><title>Multiple FadD acyl-CoA synthetases contribute to differential fatty acid degradation and virulence in Pseudomonas aeruginosa</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>A close interconnection between nutrient metabolism and virulence factor expression contributes to the pathophysiology of Pseudomonas aeruginosa as a successful pathogen. P. aeruginosa fatty acid (FA) degradation is complicated with multiple acyl-CoA synthetase homologs (FadDs) expressed in vivo in lung tissue during cystic fibrosis infections. The promoters of two genetically linked P. aeruginosa fadD genes (fadD1 and fadD2) were mapped and northern blot analysis indicated they could exist on two different transcripts. These FadDs contain ATP/AMP signature and FA-binding motifs highly homologous to those of the Escherichia coli FadD. Upon introduction into an E. coli fadD(-)/fadR(-) double mutant, both P. aeruginosa fadDs functionally complemented the E. coli fadD(-)/fadR(-) mutant, allowing degradation of different chain-length FAs. Chromosomal mutagenesis, growth analysis, induction studies, and determination of kinetic parameters suggested that FadD1 has a substrate preference for long-chain FAs while FadD2 prefers shorter-chain FAs. When compared to the wild type strain, the fadD2 mutant exhibited decreased production of lipase, protease, rhamnolipid and phospholipase, and retardation of both swimming and swarming motilities. Interestingly, fadD1 mutant showed only increased swarming motility. Growth analysis of the fadD mutants showed noticeable deficiencies in utilizing FAs and phosphatidylcholine (major components of lung surfactant) as the sole carbon source. This defect translated into decreased in vivo fitness of P. aeruginosa in a BALB/c mouse lung infection model, supporting the role of lipids as a significant nutrient source for this bacterium in vivo.</description><subject>Amino Acid Sequence</subject><subject>AMP</subject><subject>Analysis</subject><subject>Base Sequence</subject><subject>Biodegradation</subject><subject>Bioengineering</subject><subject>Biosynthesis</subject><subject>Carbon sources</subject><subject>Chains</subject><subject>Cloning</subject><subject>Coenzyme A Ligases - chemistry</subject><subject>Coenzyme A Ligases - genetics</subject><subject>Coenzyme A Ligases - metabolism</subject><subject>Cystic fibrosis</subject><subject>Degradation</subject><subject>Dehydrogenases</subject><subject>DNA, Bacterial</subject><subject>E coli</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>FADD protein</subject><subject>Fatty acids</subject><subject>Fatty Acids - metabolism</subject><subject>Fitness</subject><subject>Genes</subject><subject>Genetic aspects</subject><subject>Genetics and Genomics/Gene Expression</subject><subject>Genetics and Genomics/Gene Function</subject><subject>Genomes</subject><subject>Health aspects</subject><subject>Homology</subject><subject>Hydrolysis</subject><subject>Infections</subject><subject>Infectious Diseases/Bacterial Infections</subject><subject>Infectious Diseases/Respiratory Infections</subject><subject>Kinetics</subject><subject>Lecithin</subject><subject>Ligases</subject><subject>Lipase</subject><subject>Lipids</subject><subject>Lungs</subject><subject>Metabolism</subject><subject>Microbiology/Microbial Physiology and Metabolism</subject><subject>Molecular Sequence Data</subject><subject>Motility</subject><subject>Mutagenesis</subject><subject>Mutants</subject><subject>Mutation</subject><subject>Nutrients</subject><subject>Phosphatidylcholine</subject><subject>Phospholipase</subject><subject>Phospholipids</subject><subject>Physical fitness</subject><subject>Physiological aspects</subject><subject>Plant engineering</subject><subject>Proteases</subject><subject>Proteins</subject><subject>Pseudomonas</subject><subject>Pseudomonas aeruginosa</subject><subject>Pseudomonas aeruginosa - enzymology</subject><subject>Pseudomonas aeruginosa - pathogenicity</subject><subject>RNA, Messenger - genetics</subject><subject>Sequence Homology, Amino Acid</subject><subject>Substrate Specificity</subject><subject>Surfactants</subject><subject>Swarming</subject><subject>Swimming</subject><subject>Tuberculosis</subject><subject>Vectors (Biology)</subject><subject>Virulence</subject><subject>Virulence (Microbiology)</subject><subject>Virulence factors</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><sourceid>DOA</sourceid><recordid>eNqNk11rVDEQhg-i2Fr9B6IBQfFi15zkfN4IS7W6UKn4dRvmJJPdlGyyJjnFBX-8Wbstu9ILyUVC8rzvJJOZonha0mnJ2_LNpR-DAztde4dTSkte1-294rjsOZs0jPL7e-uj4lGMl5TWvGuah8URK2nFKtocF78_jTaZtUVyBuodAbmxk1M_I3Hj0hITRIxEepeCGcaEJHmijNYY0CUDlmhIaZNVRhGFiwAKkvGOgFPkyoTRopNIjCOfI47Kr7yDSADDuDDOR3hcPNBgIz7ZzSfF97P3304_Ts4vPsxPZ-cT2TKeJh1tkHcDwNAMdaXrqmqrrlYt0GHogXW6pvk9TV8qOjSVGlpGB93XVOuatVnJT4rn175r66PYJS6KkvWMsZ7TNhPza0J5uBTrYFYQNsKDEX83fFgICMlIi0LLoaSo-qaTQ8X7GlTfMqkBOYWeS5m93u6ijcMKlcypCmAPTA9PnFmKhb8SrK-7jvfZ4NXOIPifI8YkViZKtBYc-jGKrmUl60pWZfLFP-Tdj9tRC8j3N077HFZuPcWsanlX8YayTE3voPJQuDK5BFCbvH8geH0g2JYJ_koLGGMU869f_p-9-HHIvtxjlwg2LaO347ay4iFYXYMy-BgD6tscl1Rse-QmG2LbI2LXI1n2bP9_bkU3TcH_AAOCDdw</recordid><startdate>20101021</startdate><enddate>20101021</enddate><creator>Kang, Yun</creator><creator>Zarzycki-Siek, Jan</creator><creator>Walton, Chad B</creator><creator>Norris, Michael H</creator><creator>Hoang, Tung T</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20101021</creationdate><title>Multiple FadD acyl-CoA synthetases contribute to differential fatty acid degradation and virulence in Pseudomonas aeruginosa</title><author>Kang, Yun ; Zarzycki-Siek, Jan ; Walton, Chad B ; Norris, Michael H ; Hoang, Tung T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c723t-806e38baab6b54f5447485d7a0bb9a28f50104691d0b64db720bf950ff527e383</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Amino Acid Sequence</topic><topic>AMP</topic><topic>Analysis</topic><topic>Base Sequence</topic><topic>Biodegradation</topic><topic>Bioengineering</topic><topic>Biosynthesis</topic><topic>Carbon sources</topic><topic>Chains</topic><topic>Cloning</topic><topic>Coenzyme A Ligases - 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P. aeruginosa fatty acid (FA) degradation is complicated with multiple acyl-CoA synthetase homologs (FadDs) expressed in vivo in lung tissue during cystic fibrosis infections. The promoters of two genetically linked P. aeruginosa fadD genes (fadD1 and fadD2) were mapped and northern blot analysis indicated they could exist on two different transcripts. These FadDs contain ATP/AMP signature and FA-binding motifs highly homologous to those of the Escherichia coli FadD. Upon introduction into an E. coli fadD(-)/fadR(-) double mutant, both P. aeruginosa fadDs functionally complemented the E. coli fadD(-)/fadR(-) mutant, allowing degradation of different chain-length FAs. Chromosomal mutagenesis, growth analysis, induction studies, and determination of kinetic parameters suggested that FadD1 has a substrate preference for long-chain FAs while FadD2 prefers shorter-chain FAs. When compared to the wild type strain, the fadD2 mutant exhibited decreased production of lipase, protease, rhamnolipid and phospholipase, and retardation of both swimming and swarming motilities. Interestingly, fadD1 mutant showed only increased swarming motility. Growth analysis of the fadD mutants showed noticeable deficiencies in utilizing FAs and phosphatidylcholine (major components of lung surfactant) as the sole carbon source. This defect translated into decreased in vivo fitness of P. aeruginosa in a BALB/c mouse lung infection model, supporting the role of lipids as a significant nutrient source for this bacterium in vivo.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>21042406</pmid><doi>10.1371/journal.pone.0013557</doi><tpages>e13557</tpages><oa>free_for_read</oa></addata></record> |
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| recordid | cdi_plos_journals_1292229307 |
| source | Public Library of Science (PLoS) Journals Open Access; MEDLINE; DOAJ Directory of Open Access Journals; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence AMP Analysis Base Sequence Biodegradation Bioengineering Biosynthesis Carbon sources Chains Cloning Coenzyme A Ligases - chemistry Coenzyme A Ligases - genetics Coenzyme A Ligases - metabolism Cystic fibrosis Degradation Dehydrogenases DNA, Bacterial E coli Enzymes Escherichia coli Escherichia coli - enzymology FADD protein Fatty acids Fatty Acids - metabolism Fitness Genes Genetic aspects Genetics and Genomics/Gene Expression Genetics and Genomics/Gene Function Genomes Health aspects Homology Hydrolysis Infections Infectious Diseases/Bacterial Infections Infectious Diseases/Respiratory Infections Kinetics Lecithin Ligases Lipase Lipids Lungs Metabolism Microbiology/Microbial Physiology and Metabolism Molecular Sequence Data Motility Mutagenesis Mutants Mutation Nutrients Phosphatidylcholine Phospholipase Phospholipids Physical fitness Physiological aspects Plant engineering Proteases Proteins Pseudomonas Pseudomonas aeruginosa Pseudomonas aeruginosa - enzymology Pseudomonas aeruginosa - pathogenicity RNA, Messenger - genetics Sequence Homology, Amino Acid Substrate Specificity Surfactants Swarming Swimming Tuberculosis Vectors (Biology) Virulence Virulence (Microbiology) Virulence factors |
| title | Multiple FadD acyl-CoA synthetases contribute to differential fatty acid degradation and virulence in Pseudomonas aeruginosa |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-04T06%3A33%3A54IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Multiple%20FadD%20acyl-CoA%20synthetases%20contribute%20to%20differential%20fatty%20acid%20degradation%20and%20virulence%20in%20Pseudomonas%20aeruginosa&rft.jtitle=PloS%20one&rft.au=Kang,%20Yun&rft.date=2010-10-21&rft.volume=5&rft.issue=10&rft.spage=e13557&rft.pages=e13557-&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0013557&rft_dat=%3Cgale_plos_%3EA473843602%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1292229307&rft_id=info:pmid/21042406&rft_galeid=A473843602&rft_doaj_id=oai_doaj_org_article_fcb10ed968cb4395ad972cfae30a93cc&rfr_iscdi=true |