FNR-Dependent RmpA and RmpA2 Regulation of Capsule Polysaccharide Biosynthesis in Klebsiella pneumoniae.
Identifieur interne : 000240 ( Main/Exploration ); précédent : 000239; suivant : 000241FNR-Dependent RmpA and RmpA2 Regulation of Capsule Polysaccharide Biosynthesis in Klebsiella pneumoniae.
Auteurs : Tien-Huang Lin [Taïwan] ; Chien-Chen Wu [Taïwan] ; Jong-Tar Kuo [Taïwan] ; Hsu-Feng Chu [Taïwan] ; Ding-Yu Lee [Taïwan] ; Ching-Ting Lin [Taïwan]Source :
- Frontiers in microbiology [ 1664-302X ] ; 2019.
Abstract
Fumarate nitrate reduction regulator (FNR) is a direct oxygen-responsive transcriptional regulator containing an iron-sulfur (Fe-S) cluster. During anaerobic growth, the [4Fe-4S] cluster in FNR (holo-FNR) binds specifically to DNA, whereas exposure to oxygen results in the loss of its DNA-binding activity via oxidation of the [4Fe-4S] cluster. In this study, we aimed to investigate the role of FNR in regulation of capsular polysaccharide (CPS) biosynthesis, serum resistance, and anti-phagocytosis of K. pneumoniae. We found that the CPS amount in K. pneumoniae increased in anaerobic conditions, compared to that in aerobic conditions. An fnr deletion mutant and a site-directed mutant (fnr3CA), with the three cysteines (C20, C23, and C29) replaced with alanines to mimic an FNR lacking the [4Fe-4S] cluster, showed marked increase in CPS amount under anaerobic conditions. A promoter-reporter assay and qRT-PCR confirmed that the transcription of the cps genes was repressed by holo-FNR. In addition, we found that holo-FNR could repress the transcription of rmpA and rmpA2, encoding cps transcriptional activators. Deletion of rmpA or rmpA2 in the Δfnr strain reduced CPS biosynthesis, suggesting that RmpA and RmpA2 participated in the holo-FNR-mediated repression of cps transcription, thereby regulating the CPS amount, serum resistance, and anti-phagocytosis. Taken together, our results provided evidence that RmpA and RmpA2 participated in the holo-FNR-mediated repression of CPS biosynthesis, and resistance to the host defense in response to oxygen availability.
DOI: 10.3389/fmicb.2019.02436
PubMed: 31736888
PubMed Central: PMC6828653
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of Post-Baccalaureate Chinese Medicine, Tzu Chi University, Hualien, Taiwan.</nlm:affiliation><country xml:lang="fr">Taïwan</country><wicri:regionArea>School of Post-Baccalaureate Chinese Medicine, Tzu Chi University, Hualien</wicri:regionArea><wicri:noRegion>Hualien</wicri:noRegion></affiliation></author><author><name sortKey="Wu, Chien Chen" sort="Wu, Chien Chen" uniqKey="Wu C" first="Chien-Chen" last="Wu">Chien-Chen Wu</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Biochemistry and Molecular Biology, National Yang-Ming University, Taipei, Taiwan.</nlm:affiliation><country xml:lang="fr">Taïwan</country><wicri:regionArea>Institute of Biochemistry and Molecular Biology, National Yang-Ming University, Taipei</wicri:regionArea><wicri:noRegion>Taipei</wicri:noRegion></affiliation></author><author><name sortKey="Kuo, Jong Tar" sort="Kuo, Jong Tar" uniqKey="Kuo J" first="Jong-Tar" last="Kuo">Jong-Tar Kuo</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biological Science and Technology, China University of Science and Technology, Taipei, Taiwan.</nlm:affiliation><country xml:lang="fr">Taïwan</country><wicri:regionArea>Department of Biological Science and Technology, China University of Science and Technology, Taipei</wicri:regionArea><wicri:noRegion>Taipei</wicri:noRegion></affiliation></author><author><name sortKey="Chu, Hsu Feng" sort="Chu, Hsu Feng" uniqKey="Chu H" first="Hsu-Feng" last="Chu">Hsu-Feng Chu</name><affiliation wicri:level="1"><nlm:affiliation>Biomedical Industry Ph.D. Program, National Yang-Ming University, Taipei, Taiwan.</nlm:affiliation><country xml:lang="fr">Taïwan</country><wicri:regionArea>Biomedical Industry Ph.D. Program, National Yang-Ming University, Taipei</wicri:regionArea><wicri:noRegion>Taipei</wicri:noRegion></affiliation></author><author><name sortKey="Lee, Ding Yu" sort="Lee, Ding Yu" uniqKey="Lee D" first="Ding-Yu" last="Lee">Ding-Yu Lee</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biological Science and Technology, China University of Science and Technology, Taipei, Taiwan.</nlm:affiliation><country xml:lang="fr">Taïwan</country><wicri:regionArea>Department of Biological Science and Technology, China University of Science and Technology, Taipei</wicri:regionArea><wicri:noRegion>Taipei</wicri:noRegion></affiliation></author><author><name sortKey="Lin, Ching Ting" sort="Lin, Ching Ting" uniqKey="Lin C" first="Ching-Ting" last="Lin">Ching-Ting Lin</name><affiliation wicri:level="1"><nlm:affiliation>School of Chinese Medicine, China Medical University, Taichung, Taiwan.</nlm:affiliation><country xml:lang="fr">Taïwan</country><wicri:regionArea>School of Chinese Medicine, China Medical University, Taichung</wicri:regionArea><wicri:noRegion>Taichung</wicri:noRegion></affiliation></author></analytic><series><title level="j">Frontiers in microbiology</title><idno type="ISSN">1664-302X</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Fumarate nitrate reduction regulator (FNR) is a direct oxygen-responsive transcriptional regulator containing an iron-sulfur (Fe-S) cluster. During anaerobic growth, the [4Fe-4S] cluster in FNR (holo-FNR) binds specifically to DNA, whereas exposure to oxygen results in the loss of its DNA-binding activity via oxidation of the [4Fe-4S] cluster. In this study, we aimed to investigate the role of FNR in regulation of capsular polysaccharide (CPS) biosynthesis, serum resistance, and anti-phagocytosis of <i>K. pneumoniae</i>. We found that the CPS amount in <i>K. pneumoniae</i> increased in anaerobic conditions, compared to that in aerobic conditions. An <i>fnr</i> deletion mutant and a site-directed mutant (<i>fnr</i><sub>3</sub><sub>CA</sub>), with the three cysteines (C20, C23, and C29) replaced with alanines to mimic an FNR lacking the [4Fe-4S] cluster, showed marked increase in CPS amount under anaerobic conditions. A promoter-reporter assay and qRT-PCR confirmed that the transcription of the <i>cps</i> genes was repressed by holo-FNR. In addition, we found that holo-FNR could repress the transcription of <i>rmpA</i> and <i>rmpA2</i>, encoding <i>cps</i> transcriptional activators. Deletion of <i>rmpA</i> or <i>rmpA2</i> in the Δ<i>fnr</i> strain reduced CPS biosynthesis, suggesting that RmpA and RmpA2 participated in the holo-FNR-mediated repression of <i>cps</i> transcription, thereby regulating the CPS amount, serum resistance, and anti-phagocytosis. Taken together, our results provided evidence that RmpA and RmpA2 participated in the holo-FNR-mediated repression of CPS biosynthesis, and resistance to the host defense in response to oxygen availability.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">31736888</PMID><DateRevised><Year>2020</Year><Month>09</Month><Day>29</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Print">1664-302X</ISSN><JournalIssue CitedMedium="Print"><Volume>10</Volume><PubDate><Year>2019</Year></PubDate></JournalIssue><Title>Frontiers in microbiology</Title><ISOAbbreviation>Front Microbiol</ISOAbbreviation></Journal><ArticleTitle>FNR-Dependent RmpA and RmpA2 Regulation of Capsule Polysaccharide Biosynthesis in <i>Klebsiella pneumoniae</i>.</ArticleTitle><Pagination><MedlinePgn>2436</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.3389/fmicb.2019.02436</ELocationID><Abstract><AbstractText>Fumarate nitrate reduction regulator (FNR) is a direct oxygen-responsive transcriptional regulator containing an iron-sulfur (Fe-S) cluster. During anaerobic growth, the [4Fe-4S] cluster in FNR (holo-FNR) binds specifically to DNA, whereas exposure to oxygen results in the loss of its DNA-binding activity via oxidation of the [4Fe-4S] cluster. In this study, we aimed to investigate the role of FNR in regulation of capsular polysaccharide (CPS) biosynthesis, serum resistance, and anti-phagocytosis of <i>K. pneumoniae</i>. We found that the CPS amount in <i>K. pneumoniae</i> increased in anaerobic conditions, compared to that in aerobic conditions. An <i>fnr</i> deletion mutant and a site-directed mutant (<i>fnr</i><sub>3</sub><sub>CA</sub>), with the three cysteines (C20, C23, and C29) replaced with alanines to mimic an FNR lacking the [4Fe-4S] cluster, showed marked increase in CPS amount under anaerobic conditions. A promoter-reporter assay and qRT-PCR confirmed that the transcription of the <i>cps</i> genes was repressed by holo-FNR. In addition, we found that holo-FNR could repress the transcription of <i>rmpA</i> and <i>rmpA2</i>, encoding <i>cps</i> transcriptional activators. Deletion of <i>rmpA</i> or <i>rmpA2</i> in the Δ<i>fnr</i> strain reduced CPS biosynthesis, suggesting that RmpA and RmpA2 participated in the holo-FNR-mediated repression of <i>cps</i> transcription, thereby regulating the CPS amount, serum resistance, and anti-phagocytosis. Taken together, our results provided evidence that RmpA and RmpA2 participated in the holo-FNR-mediated repression of CPS biosynthesis, and resistance to the host defense in response to oxygen availability.</AbstractText><CopyrightInformation>Copyright © 2019 Lin, Wu, Kuo, Chu, Lee and Lin.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lin</LastName><ForeName>Tien-Huang</ForeName><Initials>TH</Initials><AffiliationInfo><Affiliation>Department of Urology, Taichung Tzu Chi Hospital, The Buddhist Tzu Chi Medical Foundation, Taichung, Taiwan.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>School of Post-Baccalaureate Chinese Medicine, Tzu Chi University, Hualien, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wu</LastName><ForeName>Chien-Chen</ForeName><Initials>CC</Initials><AffiliationInfo><Affiliation>Institute of Biochemistry and Molecular Biology, National Yang-Ming University, Taipei, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kuo</LastName><ForeName>Jong-Tar</ForeName><Initials>JT</Initials><AffiliationInfo><Affiliation>Department of Biological Science and Technology, China University of Science and Technology, Taipei, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chu</LastName><ForeName>Hsu-Feng</ForeName><Initials>HF</Initials><AffiliationInfo><Affiliation>Biomedical Industry Ph.D. Program, National Yang-Ming University, Taipei, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Ding-Yu</ForeName><Initials>DY</Initials><AffiliationInfo><Affiliation>Department of Biological Science and Technology, China University of Science and Technology, Taipei, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lin</LastName><ForeName>Ching-Ting</ForeName><Initials>CT</Initials><AffiliationInfo><Affiliation>School of Chinese Medicine, China Medical University, Taichung, Taiwan.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>10</Month><Day>29</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Front Microbiol</MedlineTA><NlmUniqueID>101548977</NlmUniqueID><ISSNLinking>1664-302X</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">FNR</Keyword><Keyword MajorTopicYN="N">Klebsiella pneumoniae</Keyword><Keyword MajorTopicYN="N">RmpA</Keyword><Keyword MajorTopicYN="N">RmpA2</Keyword><Keyword MajorTopicYN="N">capsule polysaccharide</Keyword><Keyword MajorTopicYN="N">oxygen</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>04</Month><Day>15</Day></PubMedPubDate><PubMedPubDate 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Huang" uniqKey="Lin T" first="Tien-Huang" last="Lin">Tien-Huang Lin</name><name sortKey="Wu, Chien Chen" sort="Wu, Chien Chen" uniqKey="Wu C" first="Chien-Chen" last="Wu">Chien-Chen Wu</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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