Helicobacter pylori Exploits Cholesterol-Rich Microdomains for Induction of NF-κB-Dependent Responses and Peptidoglycan Delivery in Epithelial Cells▿
Identifieur interne : 001896 ( Pmc/Corpus ); précédent : 001895; suivant : 001897Helicobacter pylori Exploits Cholesterol-Rich Microdomains for Induction of NF-κB-Dependent Responses and Peptidoglycan Delivery in Epithelial Cells▿
Auteurs : Melanie L. Hutton ; Maria Kaparakis-Liaskos ; Lorinda Turner ; Ana Cardona ; Terry Kwok ; Richard L. FerreroSource :
- Infection and Immunity [ 0019-9567 ] ; 2010.
Abstract
Infection with
Url:
DOI: 10.1128/IAI.00439-10
PubMed: 20713621
PubMed Central: 2976363
Links to Exploration step
PMC:2976363Le document en format XML
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Exploits Cholesterol-Rich Microdomains for Induction of NF-κB-Dependent Responses and Peptidoglycan Delivery in Epithelial Cells<xref ref-type="fn" rid="fn1">▿</xref>
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<author><name sortKey="Hutton, Melanie L" sort="Hutton, Melanie L" uniqKey="Hutton M" first="Melanie L." last="Hutton">Melanie L. Hutton</name>
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<author><name sortKey="Kaparakis Liaskos, Maria" sort="Kaparakis Liaskos, Maria" uniqKey="Kaparakis Liaskos M" first="Maria" last="Kaparakis-Liaskos">Maria Kaparakis-Liaskos</name>
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<author><name sortKey="Kwok, Terry" sort="Kwok, Terry" uniqKey="Kwok T" first="Terry" last="Kwok">Terry Kwok</name>
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<author><name sortKey="Ferrero, Richard L" sort="Ferrero, Richard L" uniqKey="Ferrero R" first="Richard L." last="Ferrero">Richard L. Ferrero</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main"><italic>Helicobacter pylori</italic>
Exploits Cholesterol-Rich Microdomains for Induction of NF-κB-Dependent Responses and Peptidoglycan Delivery in Epithelial Cells<xref ref-type="fn" rid="fn1">▿</xref>
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<author><name sortKey="Hutton, Melanie L" sort="Hutton, Melanie L" uniqKey="Hutton M" first="Melanie L." last="Hutton">Melanie L. Hutton</name>
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<author><name sortKey="Kaparakis Liaskos, Maria" sort="Kaparakis Liaskos, Maria" uniqKey="Kaparakis Liaskos M" first="Maria" last="Kaparakis-Liaskos">Maria Kaparakis-Liaskos</name>
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<author><name sortKey="Turner, Lorinda" sort="Turner, Lorinda" uniqKey="Turner L" first="Lorinda" last="Turner">Lorinda Turner</name>
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<author><name sortKey="Cardona, Ana" sort="Cardona, Ana" uniqKey="Cardona A" first="Ana" last="Cardona">Ana Cardona</name>
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<author><name sortKey="Kwok, Terry" sort="Kwok, Terry" uniqKey="Kwok T" first="Terry" last="Kwok">Terry Kwok</name>
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<series><title level="j">Infection and Immunity</title>
<idno type="ISSN">0019-9567</idno>
<idno type="eISSN">1098-5522</idno>
<imprint><date when="2010">2010</date>
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<front><div type="abstract" xml:lang="en"><p>Infection with <italic>Helicobacter pylori cag</italic>
pathogenicity island (<italic>cag</italic>
PAI)-positive strains is associated with more destructive tissue damage and an increased risk of severe disease. The <italic>cag</italic>
PAI encodes a type IV secretion system (TFSS) that delivers the bacterial effector molecules CagA and peptidoglycan into the host cell cytoplasm, thereby inducing responses in host cells. It was previously shown that interactions between CagL, present on the TFSS pilus, and host α<sub>5</sub>
β<sub>1</sub>
integrin molecules were critical for CagA translocation and the induction of cytoskeletal rearrangements in epithelial cells. As the α<sub>5</sub>
β<sub>1</sub>
integrin is found in cholesterol-rich microdomains (known as lipid rafts), we hypothesized that these domains may also be involved in the induction of proinflammatory responses mediated by NOD1 recognition of <italic>H. pylori</italic>
peptidoglycan. Indeed, not only did methyl-β-cyclodextrin depletion of cholesterol from cultured epithelial cells have a significant effect on the levels of NF-κB and interleukin-8 (IL-8) responses induced by <italic>H. pylori</italic>
bacteria with an intact TFSS (<italic>P</italic>
< 0.05), but it also interfered with TFSS-mediated peptidoglycan delivery to cells. Both of these effects could be restored by cholesterol replenishment of the cells. Furthermore, we demonstrated for the first time the involvement of α<sub>5</sub>
β<sub>1</sub>
integrin in the induction of proinflammatory responses by <italic>H. pylori.</italic>
Taking the results together, we propose that α<sub>5</sub>
β<sub>1</sub>
integrin, which is associated with cholesterol-rich microdomains at the host cell surface, is required for NOD1 recognition of peptidoglycan and subsequent induction of NF-κB-dependent responses to <italic>H. pylori</italic>
. These data implicate cholesterol-rich microdomains as a novel platform for TFSS-dependent delivery of bacterial products to cytosolic pathogen recognition molecules.</p>
</div>
</front>
</TEI>
<pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Infect Immun</journal-id>
<journal-id journal-id-type="publisher-id">iai</journal-id>
<journal-title-group><journal-title>Infection and Immunity</journal-title>
</journal-title-group>
<issn pub-type="ppub">0019-9567</issn>
<issn pub-type="epub">1098-5522</issn>
<publisher><publisher-name>American Society for Microbiology (ASM)</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">20713621</article-id>
<article-id pub-id-type="pmc">2976363</article-id>
<article-id pub-id-type="publisher-id">0439-10</article-id>
<article-id pub-id-type="doi">10.1128/IAI.00439-10</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Cellular Microbiology: Pathogen-Host Cell Molecular Interactions</subject>
</subj-group>
</article-categories>
<title-group><article-title><italic>Helicobacter pylori</italic>
Exploits Cholesterol-Rich Microdomains for Induction of NF-κB-Dependent Responses and Peptidoglycan Delivery in Epithelial Cells<xref ref-type="fn" rid="fn1">▿</xref>
</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Hutton</surname>
<given-names>Melanie L.</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
<xref ref-type="aff" rid="aff1">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Kaparakis-Liaskos</surname>
<given-names>Maria</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
<xref ref-type="aff" rid="aff1">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Turner</surname>
<given-names>Lorinda</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
<xref ref-type="aff" rid="aff1">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Cardona</surname>
<given-names>Ana</given-names>
</name>
<xref ref-type="aff" rid="aff1">3</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Kwok</surname>
<given-names>Terry</given-names>
</name>
<xref ref-type="aff" rid="aff1">2</xref>
<xref ref-type="aff" rid="aff1">4</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Ferrero</surname>
<given-names>Richard L.</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
<xref ref-type="aff" rid="aff1">2</xref>
<xref ref-type="corresp" rid="cor1">*</xref>
</contrib>
</contrib-group>
<aff id="aff1">Centre for Innate Immunity and Infectious Diseases, Monash Institute of Medical Research, Monash University, Clayton, Australia,<label>1</label>
Department of Microbiology, Monash University, Clayton, Australia,<label>2</label>
Unité de Recherche et d'Expertise Histotechnologie et Pathologie, Institut Pasteur, Paris, France,<label>3</label>
Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia<label>4</label>
</aff>
<author-notes><corresp id="cor1"><label>*</label>
Corresponding author. Mailing address: Centre for Innate Immunity and Infectious Diseases, Monash Institute of Medical Research, Clayton 3800, Victoria, Australia. Phone: (61) 3 9594 7221. Fax: (61) 3 9594 7211. E-mail: <email>Richard.Ferrero@monash.edu</email>
</corresp>
</author-notes>
<pub-date pub-type="ppub"><month>11</month>
<year>2010</year>
</pub-date>
<pub-date pub-type="epub"><day>16</day>
<month>8</month>
<year>2010</year>
</pub-date>
<volume>78</volume>
<issue>11</issue>
<fpage>4523</fpage>
<lpage>4531</lpage>
<history><date date-type="received"><day>28</day>
<month>4</month>
<year>2010</year>
</date>
<date date-type="rev-recd"><day>31</day>
<month>5</month>
<year>2010</year>
</date>
<date date-type="accepted"><day>6</day>
<month>8</month>
<year>2010</year>
</date>
</history>
<permissions><copyright-statement>Copyright © 2010, American Society for Microbiology</copyright-statement>
<copyright-year>2010</copyright-year>
</permissions>
<self-uri xlink:title="pdf" xlink:href="zii01110004523.pdf"></self-uri>
<abstract><p>Infection with <italic>Helicobacter pylori cag</italic>
pathogenicity island (<italic>cag</italic>
PAI)-positive strains is associated with more destructive tissue damage and an increased risk of severe disease. The <italic>cag</italic>
PAI encodes a type IV secretion system (TFSS) that delivers the bacterial effector molecules CagA and peptidoglycan into the host cell cytoplasm, thereby inducing responses in host cells. It was previously shown that interactions between CagL, present on the TFSS pilus, and host α<sub>5</sub>
β<sub>1</sub>
integrin molecules were critical for CagA translocation and the induction of cytoskeletal rearrangements in epithelial cells. As the α<sub>5</sub>
β<sub>1</sub>
integrin is found in cholesterol-rich microdomains (known as lipid rafts), we hypothesized that these domains may also be involved in the induction of proinflammatory responses mediated by NOD1 recognition of <italic>H. pylori</italic>
peptidoglycan. Indeed, not only did methyl-β-cyclodextrin depletion of cholesterol from cultured epithelial cells have a significant effect on the levels of NF-κB and interleukin-8 (IL-8) responses induced by <italic>H. pylori</italic>
bacteria with an intact TFSS (<italic>P</italic>
< 0.05), but it also interfered with TFSS-mediated peptidoglycan delivery to cells. Both of these effects could be restored by cholesterol replenishment of the cells. Furthermore, we demonstrated for the first time the involvement of α<sub>5</sub>
β<sub>1</sub>
integrin in the induction of proinflammatory responses by <italic>H. pylori.</italic>
Taking the results together, we propose that α<sub>5</sub>
β<sub>1</sub>
integrin, which is associated with cholesterol-rich microdomains at the host cell surface, is required for NOD1 recognition of peptidoglycan and subsequent induction of NF-κB-dependent responses to <italic>H. pylori</italic>
. These data implicate cholesterol-rich microdomains as a novel platform for TFSS-dependent delivery of bacterial products to cytosolic pathogen recognition molecules.</p>
</abstract>
</article-meta>
<notes><fn-group><fn><p><italic>Editor:</italic>
J. B. Bliska</p>
</fn>
</fn-group>
</notes>
</front>
</pmc>
</record>
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