The immune receptor NOD1 and kinase RIP2 interact with bacterial peptidoglycan on early endosomes to promote autophagy and inflammatory signaling.
Identifieur interne : 003777 ( PubMed/Corpus ); précédent : 003776; suivant : 003778The immune receptor NOD1 and kinase RIP2 interact with bacterial peptidoglycan on early endosomes to promote autophagy and inflammatory signaling.
Auteurs : Aaron T. Irving ; Hitomi Mimuro ; Thomas A. Kufer ; Camden Lo ; Richard Wheeler ; Lorinda J. Turner ; Belinda J. Thomas ; Christian Malosse ; Michael P. Gantier ; Linda N. Casillas ; Bartholomew J. Votta ; John Bertin ; Ivo G. Boneca ; Chihiro Sasakawa ; Dana J. Philpott ; Richard L. Ferrero ; Maria Kaparakis-LiaskosSource :
- Cell host & microbe [ 1934-6069 ] ; 2014.
English descriptors
- KwdEn :
- Animals, Autophagy, Cell Line, Endosomes (immunology), Endosomes (microbiology), Helicobacter Infections (enzymology), Helicobacter Infections (genetics), Helicobacter Infections (immunology), Helicobacter pylori (immunology), Helicobacter pylori (physiology), Humans, Mice, Nod1 Signaling Adaptor Protein (genetics), Nod1 Signaling Adaptor Protein (immunology), Peptidoglycan (immunology), Protein Binding, Pseudomonas Infections (enzymology), Pseudomonas Infections (genetics), Pseudomonas Infections (immunology), Pseudomonas aeruginosa (immunology), Pseudomonas aeruginosa (physiology), Receptor-Interacting Protein Serine-Threonine Kinase 2 (genetics), Receptor-Interacting Protein Serine-Threonine Kinase 2 (immunology), Receptors, Immunologic (genetics), Receptors, Immunologic (immunology), Signal Transduction.
- MESH :
- chemical , genetics : Nod1 Signaling Adaptor Protein, Receptor-Interacting Protein Serine-Threonine Kinase 2, Receptors, Immunologic.
- enzymology : Helicobacter Infections, Pseudomonas Infections.
- genetics : Helicobacter Infections, Pseudomonas Infections.
- immunology : Endosomes, Helicobacter Infections, Helicobacter pylori, Nod1 Signaling Adaptor Protein, Peptidoglycan, Pseudomonas Infections, Pseudomonas aeruginosa, Receptor-Interacting Protein Serine-Threonine Kinase 2, Receptors, Immunologic.
- microbiology : Endosomes.
- physiology : Helicobacter pylori, Pseudomonas aeruginosa.
- Animals, Autophagy, Cell Line, Humans, Mice, Protein Binding, Signal Transduction.
Abstract
The intracellular innate immune receptor NOD1 detects Gram-negative bacterial peptidoglycan (PG) to induce autophagy and inflammatory responses in host cells. To date, the intracellular compartment in which PG is detected by NOD1 and whether NOD1 directly interacts with PG are two questions that remain to be resolved. To address this, we used outer membrane vesicles (OMVs) from pathogenic bacteria as a physiological mechanism to deliver PG into the host cell cytosol. We report that OMVs induced autophagosome formation and inflammatory IL-8 responses in epithelial cells in a NOD1- and RIP2-dependent manner. PG contained within OMVs colocalized with both NOD1 and RIP2 in EEA1-positive early endosomes. Further, we provide evidence for direct interactions between NOD1 and PG. Collectively, these findings demonstrate that NOD1 detects PG within early endosomes, thereby promoting RIP2-dependent autophagy and inflammatory signaling in response to bacterial infection.
DOI: 10.1016/j.chom.2014.04.001
PubMed: 24746552
Links to Exploration step
pubmed:24746552Le document en format XML
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Irving</name><affiliation><nlm:affiliation>Centre for Cancer Research, Monash Institute of Medical Research, Clayton, VIC 3168, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Mimuro, Hitomi" sort="Mimuro, Hitomi" uniqKey="Mimuro H" first="Hitomi" last="Mimuro">Hitomi Mimuro</name><affiliation><nlm:affiliation>Division of Bacteriology, Department of Infectious Diseases Control, International Research Center for Infectious Diseases, Institute of Medical Science, The University of Tokyo, Tokyo 108-8639, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Kufer, Thomas A" sort="Kufer, Thomas A" uniqKey="Kufer T" first="Thomas A" last="Kufer">Thomas A. 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Boneca</name><affiliation><nlm:affiliation>Institut Pasteur, Unité Biologie et Génétique de la Paroi Bactérienne, Paris 75015, France; INSERM, Avenir group, Paris 75015, France.</nlm:affiliation></affiliation></author><author><name sortKey="Sasakawa, Chihiro" sort="Sasakawa, Chihiro" uniqKey="Sasakawa C" first="Chihiro" last="Sasakawa">Chihiro Sasakawa</name><affiliation><nlm:affiliation>Division of Bacterial Infection Biology, Institute of Medical Science, The University of Tokyo, Tokyo 108-8639, Japan; Nippon Institute for Biological Science, Tokyo 198-0024, Japan; Medical Mycology Research Center, Chiba University, Chiba 260-8673, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Philpott, Dana J" sort="Philpott, Dana J" uniqKey="Philpott D" first="Dana J" last="Philpott">Dana J. Philpott</name><affiliation><nlm:affiliation>Department of Immunology, University of Toronto, Toronto, ON M5S 1A8, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Ferrero, Richard L" sort="Ferrero, Richard L" uniqKey="Ferrero R" first="Richard L" last="Ferrero">Richard L. Ferrero</name><affiliation><nlm:affiliation>Centre for Innate Immunity and Infectious Diseases, Monash Institute of Medical Research, Clayton, VIC 3168, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Kaparakis Liaskos, Maria" sort="Kaparakis Liaskos, Maria" uniqKey="Kaparakis Liaskos M" first="Maria" last="Kaparakis-Liaskos">Maria Kaparakis-Liaskos</name><affiliation><nlm:affiliation>Centre for Innate Immunity and Infectious Diseases, Monash Institute of Medical Research, Clayton, VIC 3168, Australia. Electronic address: maria.liaskos@monash.edu.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:24746552</idno><idno type="pmid">24746552</idno><idno type="doi">10.1016/j.chom.2014.04.001</idno><idno type="wicri:Area/PubMed/Corpus">003777</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">003777</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The immune receptor NOD1 and kinase RIP2 interact with bacterial peptidoglycan on early endosomes to promote autophagy and inflammatory signaling.</title><author><name sortKey="Irving, Aaron T" sort="Irving, Aaron T" uniqKey="Irving A" first="Aaron T" last="Irving">Aaron T. Irving</name><affiliation><nlm:affiliation>Centre for Cancer Research, Monash Institute of Medical Research, Clayton, VIC 3168, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Mimuro, Hitomi" sort="Mimuro, Hitomi" uniqKey="Mimuro H" first="Hitomi" last="Mimuro">Hitomi Mimuro</name><affiliation><nlm:affiliation>Division of Bacteriology, Department of Infectious Diseases Control, International Research Center for Infectious Diseases, Institute of Medical Science, The University of Tokyo, Tokyo 108-8639, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Kufer, Thomas A" sort="Kufer, Thomas A" uniqKey="Kufer T" first="Thomas A" last="Kufer">Thomas A. Kufer</name><affiliation><nlm:affiliation>Institute for Medical Microbiology, Immunology and Hygiene, University of Cologne, Köln 50931, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Lo, Camden" sort="Lo, Camden" uniqKey="Lo C" first="Camden" last="Lo">Camden Lo</name><affiliation><nlm:affiliation>Monash Micro Imaging, Clayton, VIC 3168, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Wheeler, Richard" sort="Wheeler, Richard" uniqKey="Wheeler R" first="Richard" last="Wheeler">Richard Wheeler</name><affiliation><nlm:affiliation>Institut Pasteur, Unité Biologie et Génétique de la Paroi Bactérienne, Paris 75015, France; INSERM, Avenir group, Paris 75015, France.</nlm:affiliation></affiliation></author><author><name sortKey="Turner, Lorinda J" sort="Turner, Lorinda J" uniqKey="Turner L" first="Lorinda J" last="Turner">Lorinda J. Turner</name><affiliation><nlm:affiliation>Centre for Innate Immunity and Infectious Diseases, Monash Institute of Medical Research, Clayton, VIC 3168, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Thomas, Belinda J" sort="Thomas, Belinda J" uniqKey="Thomas B" first="Belinda J" last="Thomas">Belinda J. Thomas</name><affiliation><nlm:affiliation>Centre for Innate Immunity and Infectious Diseases, Monash Institute of Medical Research, Clayton, VIC 3168, Australia; Monash Lung and Sleep, Monash Medical Centre, Clayton, VIC 3168, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Malosse, Christian" sort="Malosse, Christian" uniqKey="Malosse C" first="Christian" last="Malosse">Christian Malosse</name><affiliation><nlm:affiliation>Institut Pasteur, Structural Mass Spectrometry and Proteomics Unit, Paris 75015, France.</nlm:affiliation></affiliation></author><author><name sortKey="Gantier, Michael P" sort="Gantier, Michael P" uniqKey="Gantier M" first="Michael P" last="Gantier">Michael P. Gantier</name><affiliation><nlm:affiliation>Centre for Cancer Research, Monash Institute of Medical Research, Clayton, VIC 3168, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Casillas, Linda N" sort="Casillas, Linda N" uniqKey="Casillas L" first="Linda N" last="Casillas">Linda N. Casillas</name><affiliation><nlm:affiliation>Pattern Recognition Receptor Discovery Performance Unit, Immuno-Inflammation Therapy Area, GlaxoSmithKline, Collegeville, PA 19426-0989, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Votta, Bartholomew J" sort="Votta, Bartholomew J" uniqKey="Votta B" first="Bartholomew J" last="Votta">Bartholomew J. Votta</name><affiliation><nlm:affiliation>Pattern Recognition Receptor Discovery Performance Unit, Immuno-Inflammation Therapy Area, GlaxoSmithKline, Collegeville, PA 19426-0989, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Bertin, John" sort="Bertin, John" uniqKey="Bertin J" first="John" last="Bertin">John Bertin</name><affiliation><nlm:affiliation>Pattern Recognition Receptor Discovery Performance Unit, Immuno-Inflammation Therapy Area, GlaxoSmithKline, Collegeville, PA 19426-0989, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Boneca, Ivo G" sort="Boneca, Ivo G" uniqKey="Boneca I" first="Ivo G" last="Boneca">Ivo G. Boneca</name><affiliation><nlm:affiliation>Institut Pasteur, Unité Biologie et Génétique de la Paroi Bactérienne, Paris 75015, France; INSERM, Avenir group, Paris 75015, France.</nlm:affiliation></affiliation></author><author><name sortKey="Sasakawa, Chihiro" sort="Sasakawa, Chihiro" uniqKey="Sasakawa C" first="Chihiro" last="Sasakawa">Chihiro Sasakawa</name><affiliation><nlm:affiliation>Division of Bacterial Infection Biology, Institute of Medical Science, The University of Tokyo, Tokyo 108-8639, Japan; Nippon Institute for Biological Science, Tokyo 198-0024, Japan; Medical Mycology Research Center, Chiba University, Chiba 260-8673, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Philpott, Dana J" sort="Philpott, Dana J" uniqKey="Philpott D" first="Dana J" last="Philpott">Dana J. Philpott</name><affiliation><nlm:affiliation>Department of Immunology, University of Toronto, Toronto, ON M5S 1A8, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Ferrero, Richard L" sort="Ferrero, Richard L" uniqKey="Ferrero R" first="Richard L" last="Ferrero">Richard L. Ferrero</name><affiliation><nlm:affiliation>Centre for Innate Immunity and Infectious Diseases, Monash Institute of Medical Research, Clayton, VIC 3168, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Kaparakis Liaskos, Maria" sort="Kaparakis Liaskos, Maria" uniqKey="Kaparakis Liaskos M" first="Maria" last="Kaparakis-Liaskos">Maria Kaparakis-Liaskos</name><affiliation><nlm:affiliation>Centre for Innate Immunity and Infectious Diseases, Monash Institute of Medical Research, Clayton, VIC 3168, Australia. Electronic address: maria.liaskos@monash.edu.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Cell host & microbe</title><idno type="eISSN">1934-6069</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Autophagy</term><term>Cell Line</term><term>Endosomes (immunology)</term><term>Endosomes (microbiology)</term><term>Helicobacter Infections (enzymology)</term><term>Helicobacter Infections (genetics)</term><term>Helicobacter Infections (immunology)</term><term>Helicobacter pylori (immunology)</term><term>Helicobacter pylori (physiology)</term><term>Humans</term><term>Mice</term><term>Nod1 Signaling Adaptor Protein (genetics)</term><term>Nod1 Signaling Adaptor Protein (immunology)</term><term>Peptidoglycan (immunology)</term><term>Protein Binding</term><term>Pseudomonas Infections (enzymology)</term><term>Pseudomonas Infections (genetics)</term><term>Pseudomonas Infections (immunology)</term><term>Pseudomonas aeruginosa (immunology)</term><term>Pseudomonas aeruginosa (physiology)</term><term>Receptor-Interacting Protein Serine-Threonine Kinase 2 (genetics)</term><term>Receptor-Interacting Protein Serine-Threonine Kinase 2 (immunology)</term><term>Receptors, Immunologic (genetics)</term><term>Receptors, Immunologic (immunology)</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Nod1 Signaling Adaptor Protein</term><term>Receptor-Interacting Protein Serine-Threonine Kinase 2</term><term>Receptors, Immunologic</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Helicobacter Infections</term><term>Pseudomonas Infections</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Helicobacter Infections</term><term>Pseudomonas Infections</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Endosomes</term><term>Helicobacter Infections</term><term>Helicobacter pylori</term><term>Nod1 Signaling Adaptor Protein</term><term>Peptidoglycan</term><term>Pseudomonas Infections</term><term>Pseudomonas aeruginosa</term><term>Receptor-Interacting Protein Serine-Threonine Kinase 2</term><term>Receptors, Immunologic</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Endosomes</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Helicobacter pylori</term><term>Pseudomonas aeruginosa</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Autophagy</term><term>Cell Line</term><term>Humans</term><term>Mice</term><term>Protein Binding</term><term>Signal Transduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The intracellular innate immune receptor NOD1 detects Gram-negative bacterial peptidoglycan (PG) to induce autophagy and inflammatory responses in host cells. To date, the intracellular compartment in which PG is detected by NOD1 and whether NOD1 directly interacts with PG are two questions that remain to be resolved. To address this, we used outer membrane vesicles (OMVs) from pathogenic bacteria as a physiological mechanism to deliver PG into the host cell cytosol. We report that OMVs induced autophagosome formation and inflammatory IL-8 responses in epithelial cells in a NOD1- and RIP2-dependent manner. PG contained within OMVs colocalized with both NOD1 and RIP2 in EEA1-positive early endosomes. Further, we provide evidence for direct interactions between NOD1 and PG. Collectively, these findings demonstrate that NOD1 detects PG within early endosomes, thereby promoting RIP2-dependent autophagy and inflammatory signaling in response to bacterial infection.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24746552</PMID><DateCreated><Year>2014</Year><Month>05</Month><Day>16</Day></DateCreated><DateCompleted><Year>2015</Year><Month>01</Month><Day>09</Day></DateCompleted><DateRevised><Year>2014</Year><Month>05</Month><Day>16</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1934-6069</ISSN><JournalIssue CitedMedium="Internet"><Volume>15</Volume><Issue>5</Issue><PubDate><Year>2014</Year><Month>May</Month><Day>14</Day></PubDate></JournalIssue><Title>Cell host & microbe</Title><ISOAbbreviation>Cell Host Microbe</ISOAbbreviation></Journal><ArticleTitle>The immune receptor NOD1 and kinase RIP2 interact with bacterial peptidoglycan on early endosomes to promote autophagy and inflammatory signaling.</ArticleTitle><Pagination><MedlinePgn>623-35</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.chom.2014.04.001</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S1931-3128(14)00135-8</ELocationID><Abstract><AbstractText>The intracellular innate immune receptor NOD1 detects Gram-negative bacterial peptidoglycan (PG) to induce autophagy and inflammatory responses in host cells. To date, the intracellular compartment in which PG is detected by NOD1 and whether NOD1 directly interacts with PG are two questions that remain to be resolved. To address this, we used outer membrane vesicles (OMVs) from pathogenic bacteria as a physiological mechanism to deliver PG into the host cell cytosol. We report that OMVs induced autophagosome formation and inflammatory IL-8 responses in epithelial cells in a NOD1- and RIP2-dependent manner. PG contained within OMVs colocalized with both NOD1 and RIP2 in EEA1-positive early endosomes. Further, we provide evidence for direct interactions between NOD1 and PG. Collectively, these findings demonstrate that NOD1 detects PG within early endosomes, thereby promoting RIP2-dependent autophagy and inflammatory signaling in response to bacterial infection.</AbstractText><CopyrightInformation>Copyright © 2014 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Irving</LastName><ForeName>Aaron T</ForeName><Initials>AT</Initials><AffiliationInfo><Affiliation>Centre for Cancer Research, Monash Institute of Medical Research, Clayton, VIC 3168, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mimuro</LastName><ForeName>Hitomi</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Division of Bacteriology, Department of Infectious Diseases Control, International Research Center for Infectious Diseases, Institute of Medical Science, The University of Tokyo, Tokyo 108-8639, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kufer</LastName><ForeName>Thomas A</ForeName><Initials>TA</Initials><AffiliationInfo><Affiliation>Institute for Medical Microbiology, Immunology and Hygiene, University of Cologne, Köln 50931, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lo</LastName><ForeName>Camden</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Monash Micro Imaging, Clayton, VIC 3168, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wheeler</LastName><ForeName>Richard</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Institut Pasteur, Unité Biologie et Génétique de la Paroi Bactérienne, Paris 75015, France; INSERM, Avenir group, Paris 75015, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Turner</LastName><ForeName>Lorinda J</ForeName><Initials>LJ</Initials><AffiliationInfo><Affiliation>Centre for Innate Immunity and Infectious Diseases, Monash Institute of Medical Research, Clayton, VIC 3168, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Thomas</LastName><ForeName>Belinda J</ForeName><Initials>BJ</Initials><AffiliationInfo><Affiliation>Centre for Innate Immunity and Infectious Diseases, Monash Institute of Medical Research, Clayton, VIC 3168, Australia; Monash Lung and Sleep, Monash Medical Centre, Clayton, VIC 3168, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Malosse</LastName><ForeName>Christian</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Institut Pasteur, Structural Mass Spectrometry and Proteomics Unit, Paris 75015, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gantier</LastName><ForeName>Michael P</ForeName><Initials>MP</Initials><AffiliationInfo><Affiliation>Centre for Cancer Research, Monash Institute of Medical Research, Clayton, VIC 3168, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Casillas</LastName><ForeName>Linda N</ForeName><Initials>LN</Initials><AffiliationInfo><Affiliation>Pattern Recognition Receptor Discovery Performance Unit, Immuno-Inflammation Therapy Area, GlaxoSmithKline, Collegeville, PA 19426-0989, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Votta</LastName><ForeName>Bartholomew J</ForeName><Initials>BJ</Initials><AffiliationInfo><Affiliation>Pattern Recognition Receptor Discovery Performance Unit, Immuno-Inflammation Therapy Area, GlaxoSmithKline, Collegeville, PA 19426-0989, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bertin</LastName><ForeName>John</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Pattern Recognition Receptor Discovery Performance Unit, Immuno-Inflammation Therapy Area, GlaxoSmithKline, Collegeville, PA 19426-0989, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Boneca</LastName><ForeName>Ivo G</ForeName><Initials>IG</Initials><AffiliationInfo><Affiliation>Institut Pasteur, Unité Biologie et Génétique de la Paroi Bactérienne, Paris 75015, France; INSERM, Avenir group, Paris 75015, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sasakawa</LastName><ForeName>Chihiro</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Division of Bacterial Infection Biology, Institute of Medical Science, The University of Tokyo, Tokyo 108-8639, Japan; Nippon Institute for Biological Science, Tokyo 198-0024, Japan; Medical Mycology Research Center, Chiba University, Chiba 260-8673, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Philpott</LastName><ForeName>Dana J</ForeName><Initials>DJ</Initials><AffiliationInfo><Affiliation>Department of Immunology, University of Toronto, Toronto, ON M5S 1A8, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ferrero</LastName><ForeName>Richard L</ForeName><Initials>RL</Initials><AffiliationInfo><Affiliation>Centre for Innate Immunity and Infectious Diseases, Monash Institute of Medical Research, Clayton, VIC 3168, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kaparakis-Liaskos</LastName><ForeName>Maria</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Centre for Innate Immunity and Infectious Diseases, Monash Institute of Medical Research, Clayton, VIC 3168, Australia. Electronic address: maria.liaskos@monash.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>04</Month><Day>17</Day></ArticleDate></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="D053474">Nod1 Signaling Adaptor Protein</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010457">Peptidoglycan</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011971">Receptors, Immunologic</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="C506253">RIPK2 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D053475">Receptor-Interacting Protein Serine-Threonine Kinase 2</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001343" MajorTopicYN="Y">Autophagy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011992" MajorTopicYN="N">Endosomes</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016481" MajorTopicYN="N">Helicobacter Infections</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016480" MajorTopicYN="N">Helicobacter pylori</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053474" MajorTopicYN="N">Nod1 Signaling Adaptor Protein</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010457" MajorTopicYN="N">Peptidoglycan</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011552" MajorTopicYN="N">Pseudomonas Infections</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011550" MajorTopicYN="N">Pseudomonas aeruginosa</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053475" MajorTopicYN="N">Receptor-Interacting Protein Serine-Threonine Kinase 2</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011971" MajorTopicYN="N">Receptors, Immunologic</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>01</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2014</Year><Month>03</Month><Day>31</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>04</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>4</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>4</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>1</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24746552</ArticleId><ArticleId IdType="pii">S1931-3128(14)00135-8</ArticleId><ArticleId IdType="doi">10.1016/j.chom.2014.04.001</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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