RapamycinFungusV1, Main, Exploration, bibRecord, 000591

Helicobacter pylori Infection Modulates Host Cell Metabolism through VacA-Dependent Inhibition of mTORC1.

Identifieur interne : 000591 ( Main/Exploration ); précédent : 000590; suivant : 000592

Helicobacter pylori Infection Modulates Host Cell Metabolism through VacA-Dependent Inhibition of mTORC1.

Auteurs : Ik-Jung Kim [États-Unis] ; Jeongmin Lee [États-Unis] ; Seung J. Oh [États-Unis] ; Mee-Sup Yoon [Corée du Sud] ; Sung-Soo Jang [États-Unis] ; Robin L. Holland [États-Unis] ; Michael L. Reno [États-Unis] ; Mohammed N. Hamad [États-Unis] ; Tatsuya Maeda [Japon] ; Hee Jung Chung [États-Unis] ; Jie Chen [États-Unis] ; Steven R. Blanke [États-Unis]

Source :

Cell host & microbe [ 1934-6069 ] ; 2018.

RBID : pubmed:29746831

Descripteurs français

English descriptors

KwdEn :
- Amino Acids (MeSH), Animals (MeSH), Autophagy (drug effects), Autophagy-Related Protein-1 Homolog (metabolism), Bacterial Proteins (metabolism), Bacterial Proteins (toxicity), Bacterial Toxins (metabolism), Cell Line (MeSH), Female (MeSH), HEK293 Cells (MeSH), Helicobacter Infections (metabolism), Helicobacter pylori (metabolism), Homeostasis (MeSH), Host-Pathogen Interactions (physiology), Humans (MeSH), Male (MeSH), Mechanistic Target of Rapamycin Complex 1 (drug effects), Mechanistic Target of Rapamycin Complex 1 (metabolism), Mice (MeSH), Mice, Inbred C57BL (MeSH), Mitochondria (drug effects), Mitochondria (metabolism), Protein-Serine-Threonine Kinases (metabolism).
MESH :
- chemical , drug effects : Mechanistic Target of Rapamycin Complex 1.
- chemical , metabolism : Autophagy-Related Protein-1 Homolog, Bacterial Proteins, Bacterial Toxins, Mechanistic Target of Rapamycin Complex 1, Protein-Serine-Threonine Kinases.
- chemical , toxicity : Bacterial Proteins.
- chemical : Amino Acids.
- drug effects : Autophagy, Mitochondria.
- metabolism : Helicobacter Infections, Helicobacter pylori, Mitochondria.
- physiology : Host-Pathogen Interactions.
- Animals, Cell Line, Female, HEK293 Cells, Homeostasis, Humans, Male, Mice, Mice, Inbred C57BL.

Abstract

Helicobacter pylori (Hp) vacuolating cytotoxin (VacA) is a bacterial exotoxin that enters host cells and induces mitochondrial dysfunction. However, the extent to which VacA-dependent mitochondrial perturbations affect overall cellular metabolism is poorly understood. We report that VacA perturbations in mitochondria are linked to alterations in cellular amino acid homeostasis, which results in the inhibition of mammalian target of rapamycin complex 1 (mTORC1) and subsequent autophagy. mTORC1, which regulates cellular metabolism during nutrient stress, is inhibited during Hp infection by a VacA-dependent mechanism. This VacA-dependent inhibition of mTORC1 signaling is linked to the dissociation of mTORC1 from the lysosomal surface and results in activation of cellular autophagy through the Unc 51-like kinase 1 (Ulk1) complex. VacA intoxication results in reduced cellular amino acids, and bolstering amino acid pools prevents VacA-mediated mTORC1 inhibition. Overall, these studies support a model that Hp modulate host cell metabolism through the action of VacA at mitochondria.

DOI: 10.1016/j.chom.2018.04.006
PubMed: 29746831
PubMed Central: PMC6538298

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000557
to stream Main, to step Curation: 000557

Le document en format XML

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<author><name sortKey="Chung, Hee Jung" sort="Chung, Hee Jung" uniqKey="Chung H" first="Hee Jung" last="Chung">Hee Jung Chung</name>
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<author><name sortKey="Maeda, Tatsuya" sort="Maeda, Tatsuya" uniqKey="Maeda T" first="Tatsuya" last="Maeda">Tatsuya Maeda</name>
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<series><title level="j">Cell host & microbe</title>
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<term>Animals (MeSH)</term>
<term>Autophagy (drug effects)</term>
<term>Autophagy-Related Protein-1 Homolog (metabolism)</term>
<term>Bacterial Proteins (metabolism)</term>
<term>Bacterial Proteins (toxicity)</term>
<term>Bacterial Toxins (metabolism)</term>
<term>Cell Line (MeSH)</term>
<term>Female (MeSH)</term>
<term>HEK293 Cells (MeSH)</term>
<term>Helicobacter Infections (metabolism)</term>
<term>Helicobacter pylori (metabolism)</term>
<term>Homeostasis (MeSH)</term>
<term>Host-Pathogen Interactions (physiology)</term>
<term>Humans (MeSH)</term>
<term>Male (MeSH)</term>
<term>Mechanistic Target of Rapamycin Complex 1 (drug effects)</term>
<term>Mechanistic Target of Rapamycin Complex 1 (metabolism)</term>
<term>Mice (MeSH)</term>
<term>Mice, Inbred C57BL (MeSH)</term>
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<term>Mitochondria (metabolism)</term>
<term>Protein-Serine-Threonine Kinases (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés (MeSH)</term>
<term>Animaux (MeSH)</term>
<term>Autophagie (effets des médicaments et des substances chimiques)</term>
<term>Cellules HEK293 (MeSH)</term>
<term>Complexe-1 cible mécanistique de la rapamycine (effets des médicaments et des substances chimiques)</term>
<term>Complexe-1 cible mécanistique de la rapamycine (métabolisme)</term>
<term>Femelle (MeSH)</term>
<term>Helicobacter pylori (métabolisme)</term>
<term>Homologue de la protéine-1 associée à l'autophagie (métabolisme)</term>
<term>Homéostasie (MeSH)</term>
<term>Humains (MeSH)</term>
<term>Infections à Helicobacter (métabolisme)</term>
<term>Interactions hôte-pathogène (physiologie)</term>
<term>Lignée cellulaire (MeSH)</term>
<term>Mitochondries (effets des médicaments et des substances chimiques)</term>
<term>Mitochondries (métabolisme)</term>
<term>Mâle (MeSH)</term>
<term>Protein-Serine-Threonine Kinases (métabolisme)</term>
<term>Protéines bactériennes (métabolisme)</term>
<term>Protéines bactériennes (toxicité)</term>
<term>Souris (MeSH)</term>
<term>Souris de lignée C57BL (MeSH)</term>
<term>Toxines bactériennes (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="drug effects" xml:lang="en"><term>Mechanistic Target of Rapamycin Complex 1</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Autophagy-Related Protein-1 Homolog</term>
<term>Bacterial Proteins</term>
<term>Bacterial Toxins</term>
<term>Mechanistic Target of Rapamycin Complex 1</term>
<term>Protein-Serine-Threonine Kinases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Bacterial Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Amino Acids</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Autophagy</term>
<term>Mitochondria</term>
</keywords>
<keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Autophagie</term>
<term>Complexe-1 cible mécanistique de la rapamycine</term>
<term>Mitochondries</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Helicobacter Infections</term>
<term>Helicobacter pylori</term>
<term>Mitochondria</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Complexe-1 cible mécanistique de la rapamycine</term>
<term>Helicobacter pylori</term>
<term>Homologue de la protéine-1 associée à l'autophagie</term>
<term>Infections à Helicobacter</term>
<term>Mitochondries</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Protéines bactériennes</term>
<term>Toxines bactériennes</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Interactions hôte-pathogène</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Host-Pathogen Interactions</term>
</keywords>
<keywords scheme="MESH" qualifier="toxicité" xml:lang="fr"><term>Protéines bactériennes</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Cell Line</term>
<term>Female</term>
<term>HEK293 Cells</term>
<term>Homeostasis</term>
<term>Humans</term>
<term>Male</term>
<term>Mice</term>
<term>Mice, Inbred C57BL</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Acides aminés</term>
<term>Animaux</term>
<term>Cellules HEK293</term>
<term>Femelle</term>
<term>Homéostasie</term>
<term>Humains</term>
<term>Lignée cellulaire</term>
<term>Mâle</term>
<term>Souris</term>
<term>Souris de lignée C57BL</term>
</keywords>
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<front><div type="abstract" xml:lang="en">Helicobacter pylori (Hp) vacuolating cytotoxin (VacA) is a bacterial exotoxin that enters host cells and induces mitochondrial dysfunction. However, the extent to which VacA-dependent mitochondrial perturbations affect overall cellular metabolism is poorly understood. We report that VacA perturbations in mitochondria are linked to alterations in cellular amino acid homeostasis, which results in the inhibition of mammalian target of rapamycin complex 1 (mTORC1) and subsequent autophagy. mTORC1, which regulates cellular metabolism during nutrient stress, is inhibited during Hp infection by a VacA-dependent mechanism. This VacA-dependent inhibition of mTORC1 signaling is linked to the dissociation of mTORC1 from the lysosomal surface and results in activation of cellular autophagy through the Unc 51-like kinase 1 (Ulk1) complex. VacA intoxication results in reduced cellular amino acids, and bolstering amino acid pools prevents VacA-mediated mTORC1 inhibition. Overall, these studies support a model that Hp modulate host cell metabolism through the action of VacA at mitochondria.</div>
</front>
</TEI>
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<DateCompleted><Year>2018</Year>
<Month>09</Month>
<Day>28</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>09</Month>
<Day>30</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1934-6069</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>23</Volume>
<Issue>5</Issue>
<PubDate><Year>2018</Year>
<Month>05</Month>
<Day>09</Day>
</PubDate>
</JournalIssue>
<Title>Cell host & microbe</Title>
<ISOAbbreviation>Cell Host Microbe</ISOAbbreviation>
</Journal>
<ArticleTitle>Helicobacter pylori Infection Modulates Host Cell Metabolism through VacA-Dependent Inhibition of mTORC1.</ArticleTitle>
<Pagination><MedlinePgn>583-593.e8</MedlinePgn>
</Pagination>
<ELocationID EIdType="pii" ValidYN="Y">S1931-3128(18)30203-8</ELocationID>
<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.chom.2018.04.006</ELocationID>
<Abstract><AbstractText>Helicobacter pylori (Hp) vacuolating cytotoxin (VacA) is a bacterial exotoxin that enters host cells and induces mitochondrial dysfunction. However, the extent to which VacA-dependent mitochondrial perturbations affect overall cellular metabolism is poorly understood. We report that VacA perturbations in mitochondria are linked to alterations in cellular amino acid homeostasis, which results in the inhibition of mammalian target of rapamycin complex 1 (mTORC1) and subsequent autophagy. mTORC1, which regulates cellular metabolism during nutrient stress, is inhibited during Hp infection by a VacA-dependent mechanism. This VacA-dependent inhibition of mTORC1 signaling is linked to the dissociation of mTORC1 from the lysosomal surface and results in activation of cellular autophagy through the Unc 51-like kinase 1 (Ulk1) complex. VacA intoxication results in reduced cellular amino acids, and bolstering amino acid pools prevents VacA-mediated mTORC1 inhibition. Overall, these studies support a model that Hp modulate host cell metabolism through the action of VacA at mitochondria.</AbstractText>
<CopyrightInformation>Copyright © 2018 Elsevier Inc. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kim</LastName>
<ForeName>Ik-Jung</ForeName>
<Initials>IJ</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology, University of Illinois, Urbana, IL 61801, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lee</LastName>
<ForeName>Jeongmin</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry, University of Illinois, Urbana, IL 61801, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Oh</LastName>
<ForeName>Seung J</ForeName>
<Initials>SJ</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry, University of Illinois, Urbana, IL 61801, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Yoon</LastName>
<ForeName>Mee-Sup</ForeName>
<Initials>MS</Initials>
<AffiliationInfo><Affiliation>Department of Cell and Developmental Biology, University of Illinois, Urbana, IL 61801, USA; Department of Molecular Medicine, School of Medicine, Gachon University, Incheon 406-840, Republic of Korea.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Jang</LastName>
<ForeName>Sung-Soo</ForeName>
<Initials>SS</Initials>
<AffiliationInfo><Affiliation>Department of Molecular and Integrative Physiology, University of Illinois, Urbana, IL 61801, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Holland</LastName>
<ForeName>Robin L</ForeName>
<Initials>RL</Initials>
<AffiliationInfo><Affiliation>Department of Pathobiology, University of Illinois, Urbana, IL 61801, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Reno</LastName>
<ForeName>Michael L</ForeName>
<Initials>ML</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology, University of Illinois, Urbana, IL 61801, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Hamad</LastName>
<ForeName>Mohammed N</ForeName>
<Initials>MN</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology, University of Illinois, Urbana, IL 61801, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Maeda</LastName>
<ForeName>Tatsuya</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>Institute of Molecular and Cellular Biosciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Chung</LastName>
<ForeName>Hee Jung</ForeName>
<Initials>HJ</Initials>
<AffiliationInfo><Affiliation>Department of Molecular and Integrative Physiology, University of Illinois, Urbana, IL 61801, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Chen</LastName>
<ForeName>Jie</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Department of Cell and Developmental Biology, University of Illinois, Urbana, IL 61801, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Blanke</LastName>
<ForeName>Steven R</ForeName>
<Initials>SR</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology, University of Illinois, Urbana, IL 61801, USA; Institute for Genomic Biology, University of Illinois, Urbana, IL 61801, USA; Lead Contact. Electronic address: sblanke@illinois.edu.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>R01 AI045928</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R01 GM089771</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R21 AI117497</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R56 AI045928</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Cell Host Microbe</MedlineTA>
<NlmUniqueID>101302316</NlmUniqueID>
<ISSNLinking>1931-3128</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000596">Amino Acids</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D001427">Bacterial Toxins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C074689">VacA protein, Helicobacter pylori</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber>
<NameOfSubstance UI="D000071189">Autophagy-Related Protein-1 Homolog</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber>
<NameOfSubstance UI="C529271">EIF2AK4 protein, human</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber>
<NameOfSubstance UI="D000076222">Mechanistic Target of Rapamycin Complex 1</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber>
<NameOfSubstance UI="D017346">Protein-Serine-Threonine Kinases</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000596" MajorTopicYN="N">Amino Acids</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001343" MajorTopicYN="N">Autophagy</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000071189" MajorTopicYN="N">Autophagy-Related Protein-1 Homolog</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000633" MajorTopicYN="Y">toxicity</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001427" MajorTopicYN="N">Bacterial Toxins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005260" MajorTopicYN="N">Female</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D057809" MajorTopicYN="N">HEK293 Cells</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016481" MajorTopicYN="N">Helicobacter Infections</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016480" MajorTopicYN="N">Helicobacter pylori</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006706" MajorTopicYN="N">Homeostasis</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D054884" MajorTopicYN="N">Host-Pathogen Interactions</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008297" MajorTopicYN="N">Male</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000076222" MajorTopicYN="N">Mechanistic Target of Rapamycin Complex 1</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008810" MajorTopicYN="N">Mice, Inbred C57BL</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008928" MajorTopicYN="N">Mitochondria</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017346" MajorTopicYN="N">Protein-Serine-Threonine Kinases</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Helicobacter pylori</Keyword>
<Keyword MajorTopicYN="Y">Ulk 1</Keyword>
<Keyword MajorTopicYN="Y">VacA</Keyword>
<Keyword MajorTopicYN="Y">amino acid homeostasis</Keyword>
<Keyword MajorTopicYN="Y">autophagy</Keyword>
<Keyword MajorTopicYN="Y">mTOR</Keyword>
<Keyword MajorTopicYN="Y">mTORC1</Keyword>
<Keyword MajorTopicYN="Y">metabolism</Keyword>
<Keyword MajorTopicYN="Y">mitochondria</Keyword>
<Keyword MajorTopicYN="Y">mitochondrial dysfunction</Keyword>
<Keyword MajorTopicYN="Y">vacuolating cytotoxin</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year>
<Month>11</Month>
<Day>24</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2018</Year>
<Month>03</Month>
<Day>15</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2018</Year>
<Month>04</Month>
<Day>17</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2018</Year>
<Month>5</Month>
<Day>11</Day>
<Hour>6</Hour>
<Minute>0</Minute>
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<PubMedPubDate PubStatus="pubmed"><Year>2018</Year>
<Month>5</Month>
<Day>11</Day>
<Hour>6</Hour>
<Minute>0</Minute>
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<PubMedPubDate PubStatus="medline"><Year>2018</Year>
<Month>10</Month>
<Day>3</Day>
<Hour>6</Hour>
<Minute>0</Minute>
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</History>
<PublicationStatus>ppublish</PublicationStatus>
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<ArticleIdList><ArticleId IdType="pubmed">9973580</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>Corée du Sud</li>
<li>Japon</li>
<li>États-Unis</li>
</country>
<region><li>Illinois</li>
<li>Région de Kantō</li>
</region>
<settlement><li>Tokyo</li>
</settlement>
<orgName><li>Université de Tokyo</li>
</orgName>
</list>
<tree><country name="États-Unis"><region name="Illinois"><name sortKey="Kim, Ik Jung" sort="Kim, Ik Jung" uniqKey="Kim I" first="Ik-Jung" last="Kim">Ik-Jung Kim</name>
</region>
<name sortKey="Blanke, Steven R" sort="Blanke, Steven R" uniqKey="Blanke S" first="Steven R" last="Blanke">Steven R. Blanke</name>
<name sortKey="Chen, Jie" sort="Chen, Jie" uniqKey="Chen J" first="Jie" last="Chen">Jie Chen</name>
<name sortKey="Chung, Hee Jung" sort="Chung, Hee Jung" uniqKey="Chung H" first="Hee Jung" last="Chung">Hee Jung Chung</name>
<name sortKey="Hamad, Mohammed N" sort="Hamad, Mohammed N" uniqKey="Hamad M" first="Mohammed N" last="Hamad">Mohammed N. Hamad</name>
<name sortKey="Holland, Robin L" sort="Holland, Robin L" uniqKey="Holland R" first="Robin L" last="Holland">Robin L. Holland</name>
<name sortKey="Jang, Sung Soo" sort="Jang, Sung Soo" uniqKey="Jang S" first="Sung-Soo" last="Jang">Sung-Soo Jang</name>
<name sortKey="Lee, Jeongmin" sort="Lee, Jeongmin" uniqKey="Lee J" first="Jeongmin" last="Lee">Jeongmin Lee</name>
<name sortKey="Oh, Seung J" sort="Oh, Seung J" uniqKey="Oh S" first="Seung J" last="Oh">Seung J. Oh</name>
<name sortKey="Reno, Michael L" sort="Reno, Michael L" uniqKey="Reno M" first="Michael L" last="Reno">Michael L. Reno</name>
</country>
<country name="Corée du Sud"><noRegion><name sortKey="Yoon, Mee Sup" sort="Yoon, Mee Sup" uniqKey="Yoon M" first="Mee-Sup" last="Yoon">Mee-Sup Yoon</name>
</noRegion>
</country>
<country name="Japon"><region name="Région de Kantō"><name sortKey="Maeda, Tatsuya" sort="Maeda, Tatsuya" uniqKey="Maeda T" first="Tatsuya" last="Maeda">Tatsuya Maeda</name>
</region>
</country>
</tree>
</affiliations>
</record>

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Helicobacter pylori Infection Modulates Host Cell Metabolism through VacA-Dependent Inhibition of mTORC1.

Helicobacter pylori Infection Modulates Host Cell Metabolism through VacA-Dependent Inhibition of mTORC1.

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