Identification of Autophagy-Inhibiting Factors of Mycobacterium tuberculosis by High-Throughput Loss-of-Function Screening.
Identifieur interne : 000111 ( Main/Exploration ); précédent : 000110; suivant : 000112Identification of Autophagy-Inhibiting Factors of Mycobacterium tuberculosis by High-Throughput Loss-of-Function Screening.
Auteurs : Emily J. Strong [États-Unis] ; Kristen L. Jurcic Smith [États-Unis] ; Neeraj K. Saini [États-Unis] ; Tony W. Ng [États-Unis] ; Steven A. Porcelli [États-Unis] ; Sunhee Lee [États-Unis]Source :
- Infection and immunity [ 1098-5522 ] ; 2020.
Abstract
The interaction of host cells with mycobacteria is complex and can lead to multiple outcomes ranging from bacterial clearance to progressive or latent infection. Autophagy is recognized as one component of host cell responses that has an essential role in innate and adaptive immunity to intracellular bacteria. Many microbes, including Mycobacterium tuberculosis, have evolved to evade or exploit autophagy, but the precise mechanisms and virulence factors are mostly unknown. Through a loss-of-function screening of an M. tuberculosis transposon mutant library, we identified 16 genes that contribute to autophagy inhibition, six of which encoded the PE/PPE protein family. Their expression in Mycobacterium smegmatis confirmed that these PE/PPE proteins inhibit autophagy and increase intracellular bacterial persistence or replication in infected cells. These effects were associated with increased mammalian target of rapamycin (mTOR) activity and also with decreased production of tumor necrosis factor alpha (TNF-α) and interleukin-1β (IL-1β). We also confirmed that the targeted deletion of the pe/ppe genes in M. tuberculosis resulted in enhanced autophagy and improved intracellular survival rates compared to those of wild-type bacteria in the infected macrophages. Differential expression of these PE/PPE proteins was observed in response to various stress conditions, suggesting that they may confer advantages to M. tuberculosis by modulating its interactions with host cells under various conditions. Our findings demonstrated that multiple M. tuberculosis PE/PPE proteins are involved in inhibiting autophagy during infection of host phagocytes and may provide strategic targets in developing therapeutics or vaccines against tuberculosis.
DOI: 10.1128/IAI.00269-20
PubMed: 32989037
Affiliations:
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Strong</name><affiliation wicri:level="2"><nlm:affiliation>Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas</wicri:regionArea><placeName><region type="state">Texas</region></placeName></affiliation></author><author><name sortKey="Jurcic Smith, Kristen L" sort="Jurcic Smith, Kristen L" uniqKey="Jurcic Smith K" first="Kristen L" last="Jurcic Smith">Kristen L. Jurcic Smith</name><affiliation wicri:level="2"><nlm:affiliation>Human Vaccine Institute, Duke University, Durham, North Carolina, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Human Vaccine Institute, Duke University, Durham, North Carolina</wicri:regionArea><placeName><region type="state">Caroline du Nord</region></placeName></affiliation></author><author><name sortKey="Saini, Neeraj K" sort="Saini, Neeraj K" uniqKey="Saini N" first="Neeraj K" last="Saini">Neeraj K. Saini</name><affiliation wicri:level="2"><nlm:affiliation>Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York</wicri:regionArea><placeName><region type="state">État de New York</region></placeName></affiliation></author><author><name sortKey="Ng, Tony W" sort="Ng, Tony W" uniqKey="Ng T" first="Tony W" last="Ng">Tony W. Ng</name><affiliation wicri:level="2"><nlm:affiliation>Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York</wicri:regionArea><placeName><region type="state">État de New York</region></placeName></affiliation></author><author><name sortKey="Porcelli, Steven A" sort="Porcelli, Steven A" uniqKey="Porcelli S" first="Steven A" last="Porcelli">Steven A. Porcelli</name><affiliation wicri:level="2"><nlm:affiliation>Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York</wicri:regionArea><placeName><region type="state">État de New York</region></placeName></affiliation><affiliation wicri:level="2"><nlm:affiliation>Department of Medicine, Albert Einstein College of Medicine, Bronx, New York, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Medicine, Albert Einstein College of Medicine, Bronx, New York</wicri:regionArea><placeName><region type="state">État de New York</region></placeName></affiliation></author><author><name sortKey="Lee, Sunhee" sort="Lee, Sunhee" uniqKey="Lee S" first="Sunhee" last="Lee">Sunhee Lee</name><affiliation wicri:level="2"><nlm:affiliation>Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas, USA sunhlee@utmb.edu.</nlm:affiliation><country wicri:rule="url">États-Unis</country><wicri:regionArea>Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas</wicri:regionArea><placeName><region type="state">Texas</region></placeName></affiliation><affiliation wicri:level="2"><nlm:affiliation>Human Vaccine Institute, Duke University, Durham, North Carolina, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Human Vaccine Institute, Duke University, Durham, North Carolina</wicri:regionArea><placeName><region type="state">Caroline du Nord</region></placeName></affiliation><affiliation wicri:level="2"><nlm:affiliation>Department of Molecular Genetics and Microbiology, Duke University, Durham, North Carolina, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular Genetics and Microbiology, Duke University, Durham, North Carolina</wicri:regionArea><placeName><region type="state">Caroline du Nord</region></placeName></affiliation></author></analytic><series><title level="j">Infection and immunity</title><idno type="eISSN">1098-5522</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The interaction of host cells with mycobacteria is complex and can lead to multiple outcomes ranging from bacterial clearance to progressive or latent infection. Autophagy is recognized as one component of host cell responses that has an essential role in innate and adaptive immunity to intracellular bacteria. Many microbes, including <i>Mycobacterium tuberculosis</i>, have evolved to evade or exploit autophagy, but the precise mechanisms and virulence factors are mostly unknown. Through a loss-of-function screening of an <i>M. tuberculosis</i> transposon mutant library, we identified 16 genes that contribute to autophagy inhibition, six of which encoded the PE/PPE protein family. Their expression in <i>Mycobacterium smegmatis</i> confirmed that these PE/PPE proteins inhibit autophagy and increase intracellular bacterial persistence or replication in infected cells. These effects were associated with increased mammalian target of rapamycin (mTOR) activity and also with decreased production of tumor necrosis factor alpha (TNF-α) and interleukin-1β (IL-1β). We also confirmed that the targeted deletion of the <i>pe</i>/<i>ppe</i> genes in <i>M. tuberculosis</i> resulted in enhanced autophagy and improved intracellular survival rates compared to those of wild-type bacteria in the infected macrophages. Differential expression of these PE/PPE proteins was observed in response to various stress conditions, suggesting that they may confer advantages to <i>M. tuberculosis</i> by modulating its interactions with host cells under various conditions. Our findings demonstrated that multiple <i>M. tuberculosis</i> PE/PPE proteins are involved in inhibiting autophagy during infection of host phagocytes and may provide strategic targets in developing therapeutics or vaccines against tuberculosis.</div></front></TEI><pubmed><MedlineCitation Status="In-Data-Review" Owner="NLM"><PMID Version="1">32989037</PMID><DateRevised><Year>2020</Year><Month>11</Month><Day>17</Day></DateRevised><Article PubModel="Electronic-Print"><Journal><ISSN IssnType="Electronic">1098-5522</ISSN><JournalIssue CitedMedium="Internet"><Volume>88</Volume><Issue>12</Issue><PubDate><Year>2020</Year><Month>Nov</Month><Day>16</Day></PubDate></JournalIssue><Title>Infection and immunity</Title><ISOAbbreviation>Infect Immun</ISOAbbreviation></Journal><ArticleTitle>Identification of Autophagy-Inhibiting Factors of Mycobacterium tuberculosis by High-Throughput Loss-of-Function Screening.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">e00269-20</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1128/IAI.00269-20</ELocationID><Abstract><AbstractText>The interaction of host cells with mycobacteria is complex and can lead to multiple outcomes ranging from bacterial clearance to progressive or latent infection. Autophagy is recognized as one component of host cell responses that has an essential role in innate and adaptive immunity to intracellular bacteria. Many microbes, including <i>Mycobacterium tuberculosis</i>, have evolved to evade or exploit autophagy, but the precise mechanisms and virulence factors are mostly unknown. Through a loss-of-function screening of an <i>M. tuberculosis</i> transposon mutant library, we identified 16 genes that contribute to autophagy inhibition, six of which encoded the PE/PPE protein family. Their expression in <i>Mycobacterium smegmatis</i> confirmed that these PE/PPE proteins inhibit autophagy and increase intracellular bacterial persistence or replication in infected cells. These effects were associated with increased mammalian target of rapamycin (mTOR) activity and also with decreased production of tumor necrosis factor alpha (TNF-α) and interleukin-1β (IL-1β). We also confirmed that the targeted deletion of the <i>pe</i>/<i>ppe</i> genes in <i>M. tuberculosis</i> resulted in enhanced autophagy and improved intracellular survival rates compared to those of wild-type bacteria in the infected macrophages. Differential expression of these PE/PPE proteins was observed in response to various stress conditions, suggesting that they may confer advantages to <i>M. tuberculosis</i> by modulating its interactions with host cells under various conditions. Our findings demonstrated that multiple <i>M. tuberculosis</i> PE/PPE proteins are involved in inhibiting autophagy during infection of host phagocytes and may provide strategic targets in developing therapeutics or vaccines against tuberculosis.</AbstractText><CopyrightInformation>Copyright © 2020 American Society for Microbiology.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Strong</LastName><ForeName>Emily J</ForeName><Initials>EJ</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jurcic Smith</LastName><ForeName>Kristen L</ForeName><Initials>KL</Initials><AffiliationInfo><Affiliation>Human Vaccine Institute, Duke University, Durham, North Carolina, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Saini</LastName><ForeName>Neeraj K</ForeName><Initials>NK</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ng</LastName><ForeName>Tony W</ForeName><Initials>TW</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Porcelli</LastName><ForeName>Steven A</ForeName><Initials>SA</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York, USA.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Medicine, Albert Einstein College of Medicine, Bronx, New York, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Sunhee</ForeName><Initials>S</Initials><Identifier Source="ORCID">https://orcid.org/0000-0002-2599-6938</Identifier><AffiliationInfo><Affiliation>Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas, USA sunhlee@utmb.edu.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Human Vaccine Institute, Duke University, Durham, North Carolina, USA.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Molecular Genetics and Microbiology, Duke University, Durham, North Carolina, USA.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 AI127711</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>11</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Infect Immun</MedlineTA><NlmUniqueID>0246127</NlmUniqueID><ISSNLinking>0019-9567</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Mycobacterium tuberculosis</Keyword><Keyword MajorTopicYN="N">PE/PPE proteins</Keyword><Keyword MajorTopicYN="N">autophagy</Keyword><Keyword MajorTopicYN="N">high-throughput screen</Keyword><Keyword MajorTopicYN="N">host-pathogen interactions</Keyword><Keyword MajorTopicYN="N">innate immunity</Keyword><Keyword MajorTopicYN="N">intracellular growth</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>05</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>09</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>9</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>9</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>9</Month><Day>29</Day><Hour>5</Hour><Minute>31</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32989037</ArticleId><ArticleId IdType="pii">IAI.00269-20</ArticleId><ArticleId IdType="doi">10.1128/IAI.00269-20</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Global tuberculosis report 2018. 2019.</Citation></Reference><Reference><Citation>Atesoh Awuh J, Flo TH. 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Jurcic Smith</name><name sortKey="Lee, Sunhee" sort="Lee, Sunhee" uniqKey="Lee S" first="Sunhee" last="Lee">Sunhee Lee</name><name sortKey="Lee, Sunhee" sort="Lee, Sunhee" uniqKey="Lee S" first="Sunhee" last="Lee">Sunhee Lee</name><name sortKey="Lee, Sunhee" sort="Lee, Sunhee" uniqKey="Lee S" first="Sunhee" last="Lee">Sunhee Lee</name><name sortKey="Ng, Tony W" sort="Ng, Tony W" uniqKey="Ng T" first="Tony W" last="Ng">Tony W. Ng</name><name sortKey="Porcelli, Steven A" sort="Porcelli, Steven A" uniqKey="Porcelli S" first="Steven A" last="Porcelli">Steven A. Porcelli</name><name sortKey="Porcelli, Steven A" sort="Porcelli, Steven A" uniqKey="Porcelli S" first="Steven A" last="Porcelli">Steven A. Porcelli</name><name sortKey="Saini, Neeraj K" sort="Saini, Neeraj K" uniqKey="Saini N" first="Neeraj K" last="Saini">Neeraj K. Saini</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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