The Shigella type three secretion system effector OspG directly and specifically binds to host ubiquitin for activation
The genus Shigella infects human gut epithelial cells to cause diarrhea and gastrointestinal disorders. Like many other Gram-negative bacterial pathogens, the virulence of Shigella spp. relies on a conserved type three secretion system that delivers a handful of effector proteins into host cells to...
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| description | The genus Shigella infects human gut epithelial cells to cause diarrhea and gastrointestinal disorders. Like many other Gram-negative bacterial pathogens, the virulence of Shigella spp. relies on a conserved type three secretion system that delivers a handful of effector proteins into host cells to manipulate various host cell physiology. However, many of the Shigella type III effectors remain functionally uncharacterized. Here we observe that OspG, one of the Shigella effectors, interacted with ubiquitin conjugates and poly-ubiquitin chains of either K48 or K63 linkage in eukaryotic host cells. Purified OspG protein formed a stable complex with ubiquitin but showed no interactions with other ubiquitin-like proteins. OspG binding to ubiquitin required the carboxyl terminal helical region in OspG and the canonical I44-centered hydrophobic surface in ubiquitin. OspG and OspG-homologous effectors, NleH1/2 from enteropathogenic E coli (EPEC), contain sub-domains I-VII of eukaryotic serine/threonine kinase. GST-tagged OspG and NleH1/2 could undergo autophosphorylation, the former of which was significantly stimulated by ubiquitin binding. Ubiquitin binding was also required for OspG functioning in attenuating host NF-κB signaling. Our data illustrate a new mechanism that bacterial pathogen like Shigella exploits ubiquitin binding to activate its secreted virulence effector for its functioning in host eukaryotic cells. |
| doi_str_mv | 10.1371/journal.pone.0057558 |
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Like many other Gram-negative bacterial pathogens, the virulence of Shigella spp. relies on a conserved type three secretion system that delivers a handful of effector proteins into host cells to manipulate various host cell physiology. However, many of the Shigella type III effectors remain functionally uncharacterized. Here we observe that OspG, one of the Shigella effectors, interacted with ubiquitin conjugates and poly-ubiquitin chains of either K48 or K63 linkage in eukaryotic host cells. Purified OspG protein formed a stable complex with ubiquitin but showed no interactions with other ubiquitin-like proteins. OspG binding to ubiquitin required the carboxyl terminal helical region in OspG and the canonical I44-centered hydrophobic surface in ubiquitin. OspG and OspG-homologous effectors, NleH1/2 from enteropathogenic E coli (EPEC), contain sub-domains I-VII of eukaryotic serine/threonine kinase. GST-tagged OspG and NleH1/2 could undergo autophosphorylation, the former of which was significantly stimulated by ubiquitin binding. Ubiquitin binding was also required for OspG functioning in attenuating host NF-κB signaling. Our data illustrate a new mechanism that bacterial pathogen like Shigella exploits ubiquitin binding to activate its secreted virulence effector for its functioning in host eukaryotic cells.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0057558</identifier><identifier>PMID: 23469023</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino Acid Sequence ; Bacteria ; Bacterial Proteins - chemistry ; Bacterial Proteins - metabolism ; Binding ; Biochemistry ; Biology ; Cell cycle ; Diarrhea ; E coli ; Effector cells ; Effectors ; Electrophoresis, Polyacrylamide Gel ; Enzymes ; Epithelial cells ; Gastrointestinal diseases ; Gene expression ; Gram-negative bacteria ; Homology ; Humans ; Hydrophobicity ; Infections ; Kinases ; Mitogen-Activated Protein Kinase 10 - chemistry ; Molecular Sequence Data ; NF-kappa B - metabolism ; NF-κB protein ; Pathogens ; Protein Binding ; Protein-serine/threonine kinase ; Proteins ; Sequence Homology, Amino Acid ; Shigella ; Shigella - metabolism ; Shigella - physiology ; Signal Transduction ; Signaling ; Threonine ; Ubiquitin ; Ubiquitin - metabolism ; Virulence ; Yersinia</subject><ispartof>PloS one, 2013-02, Vol.8 (2), p.e57558-e57558</ispartof><rights>2013 Zhou et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2013 Zhou et al 2013 Zhou et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c592t-2606aa8b0cdf5f9c66b96e741ff847f8c576a179bd3285930f550c8610d567543</citedby><cites>FETCH-LOGICAL-c592t-2606aa8b0cdf5f9c66b96e741ff847f8c576a179bd3285930f550c8610d567543</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3585378/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3585378/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79343,79344</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23469023$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Kwaik, Yousef Abu</contributor><creatorcontrib>Zhou, Yan</creatorcontrib><creatorcontrib>Dong, Na</creatorcontrib><creatorcontrib>Hu, Liyan</creatorcontrib><creatorcontrib>Shao, Feng</creatorcontrib><title>The Shigella type three secretion system effector OspG directly and specifically binds to host ubiquitin for activation</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>The genus Shigella infects human gut epithelial cells to cause diarrhea and gastrointestinal disorders. Like many other Gram-negative bacterial pathogens, the virulence of Shigella spp. relies on a conserved type three secretion system that delivers a handful of effector proteins into host cells to manipulate various host cell physiology. However, many of the Shigella type III effectors remain functionally uncharacterized. Here we observe that OspG, one of the Shigella effectors, interacted with ubiquitin conjugates and poly-ubiquitin chains of either K48 or K63 linkage in eukaryotic host cells. Purified OspG protein formed a stable complex with ubiquitin but showed no interactions with other ubiquitin-like proteins. OspG binding to ubiquitin required the carboxyl terminal helical region in OspG and the canonical I44-centered hydrophobic surface in ubiquitin. OspG and OspG-homologous effectors, NleH1/2 from enteropathogenic E coli (EPEC), contain sub-domains I-VII of eukaryotic serine/threonine kinase. GST-tagged OspG and NleH1/2 could undergo autophosphorylation, the former of which was significantly stimulated by ubiquitin binding. Ubiquitin binding was also required for OspG functioning in attenuating host NF-κB signaling. Our data illustrate a new mechanism that bacterial pathogen like Shigella exploits ubiquitin binding to activate its secreted virulence effector for its functioning in host eukaryotic cells.</description><subject>Amino Acid Sequence</subject><subject>Bacteria</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Binding</subject><subject>Biochemistry</subject><subject>Biology</subject><subject>Cell cycle</subject><subject>Diarrhea</subject><subject>E coli</subject><subject>Effector cells</subject><subject>Effectors</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzymes</subject><subject>Epithelial cells</subject><subject>Gastrointestinal diseases</subject><subject>Gene expression</subject><subject>Gram-negative bacteria</subject><subject>Homology</subject><subject>Humans</subject><subject>Hydrophobicity</subject><subject>Infections</subject><subject>Kinases</subject><subject>Mitogen-Activated Protein Kinase 10 - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhou, Yan</au><au>Dong, Na</au><au>Hu, Liyan</au><au>Shao, Feng</au><au>Kwaik, Yousef Abu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Shigella type three secretion system effector OspG directly and specifically binds to host ubiquitin for activation</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2013-02-28</date><risdate>2013</risdate><volume>8</volume><issue>2</issue><spage>e57558</spage><epage>e57558</epage><pages>e57558-e57558</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>The genus Shigella infects human gut epithelial cells to cause diarrhea and gastrointestinal disorders. Like many other Gram-negative bacterial pathogens, the virulence of Shigella spp. relies on a conserved type three secretion system that delivers a handful of effector proteins into host cells to manipulate various host cell physiology. However, many of the Shigella type III effectors remain functionally uncharacterized. Here we observe that OspG, one of the Shigella effectors, interacted with ubiquitin conjugates and poly-ubiquitin chains of either K48 or K63 linkage in eukaryotic host cells. Purified OspG protein formed a stable complex with ubiquitin but showed no interactions with other ubiquitin-like proteins. OspG binding to ubiquitin required the carboxyl terminal helical region in OspG and the canonical I44-centered hydrophobic surface in ubiquitin. OspG and OspG-homologous effectors, NleH1/2 from enteropathogenic E coli (EPEC), contain sub-domains I-VII of eukaryotic serine/threonine kinase. GST-tagged OspG and NleH1/2 could undergo autophosphorylation, the former of which was significantly stimulated by ubiquitin binding. Ubiquitin binding was also required for OspG functioning in attenuating host NF-κB signaling. Our data illustrate a new mechanism that bacterial pathogen like Shigella exploits ubiquitin binding to activate its secreted virulence effector for its functioning in host eukaryotic cells.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>23469023</pmid><doi>10.1371/journal.pone.0057558</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Bacteria Bacterial Proteins - chemistry Bacterial Proteins - metabolism Binding Biochemistry Biology Cell cycle Diarrhea E coli Effector cells Effectors Electrophoresis, Polyacrylamide Gel Enzymes Epithelial cells Gastrointestinal diseases Gene expression Gram-negative bacteria Homology Humans Hydrophobicity Infections Kinases Mitogen-Activated Protein Kinase 10 - chemistry Molecular Sequence Data NF-kappa B - metabolism NF-κB protein Pathogens Protein Binding Protein-serine/threonine kinase Proteins Sequence Homology, Amino Acid Shigella Shigella - metabolism Shigella - physiology Signal Transduction Signaling Threonine Ubiquitin Ubiquitin - metabolism Virulence Yersinia |
| title | The Shigella type three secretion system effector OspG directly and specifically binds to host ubiquitin for activation |
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