Molecular mimicry by an F-box effector of Legionella pneumophila hijacks a conserved polyubiquitination machinery within macrophages and protozoa
The ability of Legionella pneumophila to proliferate within various protozoa in the aquatic environment and in macrophages indicates a remarkable evolution and microbial exploitation of evolutionarily conserved eukaryotic processes. Ankyrin B (AnkB) of L. pneumophila is a non-canonical F-box-contain...
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Published in | PLoS pathogens Vol. 5; no. 12; p. e1000704 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Public Library of Science
01.12.2009
Public Library of Science (PLoS) |
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Abstract | The ability of Legionella pneumophila to proliferate within various protozoa in the aquatic environment and in macrophages indicates a remarkable evolution and microbial exploitation of evolutionarily conserved eukaryotic processes. Ankyrin B (AnkB) of L. pneumophila is a non-canonical F-box-containing protein, and is the only known Dot/Icm-translocated effector of L. pneumophila essential for intra-vacuolar proliferation within both macrophages and protozoan hosts. We show that the F-box domain of AnkB and the (9)L(10)P conserved residues are essential for intracellular bacterial proliferation and for rapid acquisition of polyubiquitinated proteins by the Legionella-containing vacuole (LCV) within macrophages, Dictyostelium discoideum, and Acanthamoeba. Interestingly, translocation of AnkB and recruitment of polyubiquitinated proteins in macrophages and Acanthamoeba is rapidly triggered by extracellular bacteria within 5 min of bacterial attachment. Ectopically expressed AnkB within mammalian cells is localized to the periphery of the cell where it co-localizes with host SKP1 and recruits polyubiquitinated proteins, which results in restoration of intracellular growth to the ankB mutant similar to the parental strain. While an ectopically expressed AnkB-(9)L(10)P/AA variant is localized to the cell periphery, it does not recruit polyubiquitinated proteins and fails to trans-rescue the ankB mutant intracellular growth defect. Direct in vivo interaction of AnkB but not the AnkB-(9)L(10)P/AA variant with the host SKP1 is demonstrated. Importantly, RNAi-mediated silencing of expression of SKP1 renders the cells non-permissive for intracellular proliferation of L. pneumophila. The role of AnkB in exploitation of the polyubiquitination machinery is essential for intrapulmonary bacterial proliferation in the mouse model of Legionnaires' disease. Therefore, AnkB exhibits a novel molecular and functional mimicry of eukaryotic F-box proteins that exploits conserved polyubiquitination machinery for intracellular proliferation within evolutionarily distant hosts. |
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AbstractList | The ability of Legionella pneumophila to proliferate within various protozoa in the aquatic environment and in macrophages indicates a remarkable evolution and microbial exploitation of evolutionarily conserved eukaryotic processes. Ankyrin B (AnkB) of L. pneumophila is a non-canonical F-box-containing protein, and is the only known Dot/Icm-translocated effector of L. pneumophila essential for intra-vacuolar proliferation within both macrophages and protozoan hosts. We show that the F-box domain of AnkB and the 9L10P conserved residues are essential for intracellular bacterial proliferation and for rapid acquisition of polyubiquitinated proteins by the Legionella-containing vacuole (LCV) within macrophages, Dictyostelium discoideum, and Acanthamoeba. Interestingly, translocation of AnkB and recruitment of polyubiquitinated proteins in macrophages and Acanthamoeba is rapidly triggered by extracellular bacteria within 5 min of bacterial attachment. Ectopically expressed AnkB within mammalian cells is localized to the periphery of the cell where it co-localizes with host SKP1 and recruits polyubiquitinated proteins, which results in restoration of intracellular growth to the ankB mutant similar to the parental strain. While an ectopically expressed AnkB-9L10P/AA variant is localized to the cell periphery, it does not recruit polyubiquitinated proteins and fails to trans-rescue the ankB mutant intracellular growth defect. Direct in vivo interaction of AnkB but not the AnkB-9L10P/AA variant with the host SKP1 is demonstrated. Importantly, RNAi-mediated silencing of expression of SKP1 renders the cells non-permissive for intracellular proliferation of L. pneumophila. The role of AnkB in exploitation of the polyubiquitination machinery is essential for intrapulmonary bacterial proliferation in the mouse model of Legionnaires' disease. Therefore, AnkB exhibits a novel molecular and functional mimicry of eukaryotic F-box proteins that exploits conserved polyubiquitination machinery for intracellular proliferation within evolutionarily distant hosts. Legionella pneumophila is abundantly found in the aquatic environment within various protozoa and can cause a severe pneumonia called Legionnaires' disease when it invades human macrophages in the lung. The ability of L. pneumophila to invade and proliferate within macrophages and protozoa is dependent on the translocation of specific proteins into the invaded cell via a specialized secretory device, and these proteins modulate various host cell processes. Of these translocated proteins, AnkB is indispensable for intracellular growth of L. pneumophila within macrophages and protozoa. Here we show that AnkB is essential for establishing a favorable intracellular replicative niche by promoting the decoration of the Legionella containing vacuole (LCV) with polyubiquitinated proteins. The AnkB effector achieves this by mimicking the action of host cell F-box proteins, a highly conserved component of the SCF ubiquitin ligase complex that is found in both unicellular organisms and mammalian cells. Our study provides new insights into the ability of intracellular pathogens to hijack evolutionarily conserved host cell processes through molecular mimicry to establish a favorable replicative niche within various hosts and to cause disease in mammals. The ability of Legionella pneumophila to proliferate within various protozoa in the aquatic environment and in macrophages indicates a remarkable evolution and microbial exploitation of evolutionarily conserved eukaryotic processes. Ankyrin B (AnkB) of L. pneumophila is a non-canonical F-box-containing protein, and is the only known Dot/Icm-translocated effector of L. pneumophila essential for intra-vacuolar proliferation within both macrophages and protozoan hosts. We show that the F-box domain of AnkB and the (9)L(10)P conserved residues are essential for intracellular bacterial proliferation and for rapid acquisition of polyubiquitinated proteins by the Legionella-containing vacuole (LCV) within macrophages, Dictyostelium discoideum, and Acanthamoeba. Interestingly, translocation of AnkB and recruitment of polyubiquitinated proteins in macrophages and Acanthamoeba is rapidly triggered by extracellular bacteria within 5 min of bacterial attachment. Ectopically expressed AnkB within mammalian cells is localized to the periphery of the cell where it co-localizes with host SKP1 and recruits polyubiquitinated proteins, which results in restoration of intracellular growth to the ankB mutant similar to the parental strain. While an ectopically expressed AnkB-(9)L(10)P/AA variant is localized to the cell periphery, it does not recruit polyubiquitinated proteins and fails to trans-rescue the ankB mutant intracellular growth defect. Direct in vivo interaction of AnkB but not the AnkB-(9)L(10)P/AA variant with the host SKP1 is demonstrated. Importantly, RNAi-mediated silencing of expression of SKP1 renders the cells non-permissive for intracellular proliferation of L. pneumophila. The role of AnkB in exploitation of the polyubiquitination machinery is essential for intrapulmonary bacterial proliferation in the mouse model of Legionnaires' disease. Therefore, AnkB exhibits a novel molecular and functional mimicry of eukaryotic F-box proteins that exploits conserved polyubiquitination machinery for intracellular proliferation within evolutionarily distant hosts. The ability of Legionella pneumophila to proliferate within various protozoa in the aquatic environment and in macrophages indicates a remarkable evolution and microbial exploitation of evolutionarily conserved eukaryotic processes. Ankyrin B (AnkB) of L. pneumophila is a non-canonical F-box-containing protein, and is the only known Dot/Icm-translocated effector of L. pneumophila essential for intra-vacuolar proliferation within both macrophages and protozoan hosts. We show that the F-box domain of AnkB and the 9 L 10 P conserved residues are essential for intracellular bacterial proliferation and for rapid acquisition of polyubiquitinated proteins by the Legionella -containing vacuole (LCV) within macrophages, Dictyostelium discoideum , and Acanthamoeba . Interestingly, translocation of AnkB and recruitment of polyubiquitinated proteins in macrophages and Acanthamoeba is rapidly triggered by extracellular bacteria within 5 min of bacterial attachment. Ectopically expressed AnkB within mammalian cells is localized to the periphery of the cell where it co-localizes with host SKP1 and recruits polyubiquitinated proteins, which results in restoration of intracellular growth to the ankB mutant similar to the parental strain. While an ectopically expressed AnkB- 9 L 10 P/AA variant is localized to the cell periphery, it does not recruit polyubiquitinated proteins and fails to trans-rescue the ankB mutant intracellular growth defect. Direct in vivo interaction of AnkB but not the AnkB- 9 L 10 P/AA variant with the host SKP1 is demonstrated. Importantly, RNAi-mediated silencing of expression of SKP1 renders the cells non-permissive for intracellular proliferation of L. pneumophila . The role of AnkB in exploitation of the polyubiquitination machinery is essential for intrapulmonary bacterial proliferation in the mouse model of Legionnaires' disease. Therefore, AnkB exhibits a novel molecular and functional mimicry of eukaryotic F-box proteins that exploits conserved polyubiquitination machinery for intracellular proliferation within evolutionarily distant hosts. Legionella pneumophila is abundantly found in the aquatic environment within various protozoa and can cause a severe pneumonia called Legionnaires' disease when it invades human macrophages in the lung. The ability of L. pneumophila to invade and proliferate within macrophages and protozoa is dependent on the translocation of specific proteins into the invaded cell via a specialized secretory device, and these proteins modulate various host cell processes. Of these translocated proteins, AnkB is indispensable for intracellular growth of L. pneumophila within macrophages and protozoa. Here we show that AnkB is essential for establishing a favorable intracellular replicative niche by promoting the decoration of the Legionella containing vacuole (LCV) with polyubiquitinated proteins. The AnkB effector achieves this by mimicking the action of host cell F-box proteins, a highly conserved component of the SCF ubiquitin ligase complex that is found in both unicellular organisms and mammalian cells. Our study provides new insights into the ability of intracellular pathogens to hijack evolutionarily conserved host cell processes through molecular mimicry to establish a favorable replicative niche within various hosts and to cause disease in mammals. The ability of Legionella pneumophila to proliferate within various protozoa in the aquatic environment and in macrophages indicates a remarkable evolution and microbial exploitation of evolutionarily conserved eukaryotic processes. Ankyrin B (AnkB) of L. pneumophila is a non-canonical F-box-containing protein, and is the only known Dot/Icm-translocated effector of L. pneumophila essential for intra-vacuolar proliferation within both macrophages and protozoan hosts. We show that the F-box domain of AnkB and the 9L10P conserved residues are essential for intracellular bacterial proliferation and for rapid acquisition of polyubiquitinated proteins by the Legionella-containing vacuole (LCV) within macrophages, Dictyostelium discoideum, and Acanthamoeba. Interestingly, translocation of AnkB and recruitment of polyubiquitinated proteins in macrophages and Acanthamoeba is rapidly triggered by extracellular bacteria within 5 min of bacterial attachment. Ectopically expressed AnkB within mammalian cells is localized to the periphery of the cell where it co-localizes with host SKP1 and recruits polyubiquitinated proteins, which results in restoration of intracellular growth to the ankB mutant similar to the parental strain. While an ectopically expressed AnkB-9L10P/AA variant is localized to the cell periphery, it does not recruit polyubiquitinated proteins and fails to trans-rescue the ankB mutant intracellular growth defect. Direct in vivo interaction of AnkB but not the AnkB-9L10P/AA variant with the host SKP1 is demonstrated. Importantly, RNAi-mediated silencing of expression of SKP1 renders the cells non-permissive for intracellular proliferation of L. pneumophila. The role of AnkB in exploitation of the polyubiquitination machinery is essential for intrapulmonary bacterial proliferation in the mouse model of Legionnaires' disease. Therefore, AnkB exhibits a novel molecular and functional mimicry of eukaryotic F-box proteins that exploits conserved polyubiquitination machinery for intracellular proliferation within evolutionarily distant hosts. The ability of Legionella pneumophila to proliferate within various protozoa in the aquatic environment and in macrophages indicates a remarkable evolution and microbial exploitation of evolutionarily conserved eukaryotic processes. Ankyrin B (AnkB) of L. pneumophila is a non-canonical F-box-containing protein, and is the only known Dot/Icm-translocated effector of L. pneumophila essential for intra-vacuolar proliferation within both macrophages and protozoan hosts. We show that the F-box domain of AnkB and the [sup.9]L [sup.10]P conserved residues are essential for intracellular bacterial proliferation and for rapid acquisition of polyubiquitinated proteins by the Legionella-containing vacuole (LCV) within macrophages, Dictyostelium discoideum, and Acanthamoeba. Interestingly, translocation of AnkB and recruitment of polyubiquitinated proteins in macrophages and Acanthamoeba is rapidly triggered by extracellular bacteria within 5 min of bacterial attachment. Ectopically expressed AnkB within mammalian cells is localized to the periphery of the cell where it co-localizes with host SKP1 and recruits polyubiquitinated proteins, which results in restoration of intracellular growth to the ank8 mutant similar to the parental strain. While an ectopically expressed AnkB-[sup.9]L [sup.10]P/AA variant is localized to the cell periphery, it does not recruit polyubiquitinated proteins and fails to trans-rescue the ank8 mutant intracellular growth defect. Direct in vivo interaction of AnkB but not the AnkB [sup.9]L [sup.10]P/AA variant with the host SKP1 is demonstrated. Importantly, RNAi-mediated silencing of expression of SKP1 renders the cells non-permissive for intracellular proliferation of L. pneumophila. The role of AnkB in exploitation of the polyubiquitination machinery is essential for intrapulmonary bacterial proliferation in the mouse model of Legionnaires' disease. Therefore, AnkB exhibits a novel molecular and functional mimicry of eukaryotic F-box proteins that exploits conserved polyubiquitination machinery for intracellular proliferation within evolutionarily distant hosts. |
Audience | Academic |
Author | Habyarimana, Fabien Kwaik, Yousef Abu Al-Khodor, Souhaila Santic, Marina Kalia, Awdhesh Price, Christopher T Al-Quadan, Tasneem |
AuthorAffiliation | 3 Department of Biology, University of Louisville, Kentucky, United States of America Ohio State University, United States of America 2 Department of Microbiology, University of Rijeka, Rijeka, Croatia 1 Department of Microbiology and Immunology, College of Medicine, University of Louisville, Kentucky, United States of America |
AuthorAffiliation_xml | – name: 2 Department of Microbiology, University of Rijeka, Rijeka, Croatia – name: 3 Department of Biology, University of Louisville, Kentucky, United States of America – name: 1 Department of Microbiology and Immunology, College of Medicine, University of Louisville, Kentucky, United States of America – name: Ohio State University, United States of America |
Author_xml | – sequence: 1 givenname: Christopher T surname: Price fullname: Price, Christopher T organization: Department of Microbiology and Immunology, College of Medicine, University of Louisville, Kentucky, USA – sequence: 2 givenname: Souhaila surname: Al-Khodor fullname: Al-Khodor, Souhaila – sequence: 3 givenname: Tasneem surname: Al-Quadan fullname: Al-Quadan, Tasneem – sequence: 4 givenname: Marina surname: Santic fullname: Santic, Marina – sequence: 5 givenname: Fabien surname: Habyarimana fullname: Habyarimana, Fabien – sequence: 6 givenname: Awdhesh surname: Kalia fullname: Kalia, Awdhesh – sequence: 7 givenname: Yousef Abu surname: Kwaik fullname: Kwaik, Yousef Abu |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/20041211$$D View this record in MEDLINE/PubMed |
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Cites_doi | 10.1111/j.1462-5822.2008.01251.x 10.1016/S0378-1119(97)00194-7 10.1146/annurev.cellbio.22.010605.093503 10.3109/10425179109039687 10.1038/nrm1547 10.1111/j.1462-5822.2008.01145.x 10.1016/j.tcb.2004.11.005 10.1038/35042620 10.1046/j.1365-2958.2003.03400.x 10.1128/IAI.01278-06 10.1128/IAI.00147-07 10.1111/j.1365-2958.2008.06124.x 10.1091/mbc.E06-02-0145 10.1101/gad.12.22.3564 10.1073/pnas.0802042105 10.1016/S0968-0004(99)01384-5 10.1371/journal.ppat.0020034 10.1126/science.279.5352.873 10.1038/nrmicro1967 10.1073/pnas.95.4.1669 10.1038/ng1447 10.1128/JB.187.22.7716-7726.2005 10.1016/S0959-440X(01)00266-4 10.1073/pnas.97.7.3292 10.1101/gad.871101 10.1093/nar/gkh377 10.1083/jcb.145.5.933 10.1016/S0167-4781(96)00185-6 10.1074/jbc.273.29.18242 10.1016/j.bbamcr.2004.09.027 10.1074/jbc.M410820200 10.1111/j.1462-2920.2007.01560.x 10.1371/journal.ppat.1000117 10.1111/j.1365-2958.2008.06453.x 10.1128/AEM.71.1.20-28.2005 10.1078/143446103322454158 |
ContentType | Journal Article |
Copyright | COPYRIGHT 2009 Public Library of Science Price et al. 2009 2009 Price et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Price CT, Al-Khodor S, Al-Quadan T, Santic M, Habyarimana F, et al. (2009) Molecular Mimicry by an F-Box Effector of Legionella pneumophila Hijacks a Conserved Polyubiquitination Machinery within Macrophages and Protozoa. PLoS Pathog 5(12): e1000704. doi:10.1371/journal.ppat.1000704 |
Copyright_xml | – notice: COPYRIGHT 2009 Public Library of Science – notice: Price et al. 2009 – notice: 2009 Price et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Price CT, Al-Khodor S, Al-Quadan T, Santic M, Habyarimana F, et al. (2009) Molecular Mimicry by an F-Box Effector of Legionella pneumophila Hijacks a Conserved Polyubiquitination Machinery within Macrophages and Protozoa. PLoS Pathog 5(12): e1000704. doi:10.1371/journal.ppat.1000704 |
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DocumentTitleAlternate | L. pneumophila F-Box Effector |
EISSN | 1553-7374 |
Editor | Amer, Amal O. |
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Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Conceived and designed the experiments: CTP SAK TAQ MS AK YAK. Performed the experiments: CTP SAK TAQ MS FH. Analyzed the data: CTP SAK TAQ MS FH AK YAK. Contributed reagents/materials/analysis tools: FH. Wrote the paper: CTP SAK TAQ AK YAK. |
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References | 17420236 - Infect Immun. 2007 Jun;75(6):2903-13 12675793 - Mol Microbiol. 2003 Apr;48(2):305-21 14658498 - Protist. 2003 Oct;154(3-4):419-29 11751054 - Curr Opin Struct Biol. 2001 Dec;11(6):725-32 9116025 - Biochim Biophys Acta. 1997 Mar 20;1351(1-2):126-36 9373134 - Gene. 1997 Oct 24;200(1-2):1-10 15571813 - Biochim Biophys Acta. 2004 Nov 29;1695(1-3):133-70 15653071 - Trends Cell Biol. 2005 Jan;15(1):2-5 10725352 - Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3292-7 15640165 - Appl Environ Microbiol. 2005 Jan;71(1):20-8 1667985 - DNA Seq. 1991;2(3):173-80 11099048 - Nature. 2000 Nov 16;408(6810):381-6 16652170 - PLoS Pathog. 2006 Apr;2(4):e34 16790494 - Mol Biol Cell. 2006 Sep;17(9):3756-67 16753028 - Annu Rev Cell Dev Biol. 2006;22:159-80 9832508 - Genes Dev. 1998 Nov 15;12(22):3564-78 19011659 - Nat Rev Microbiol. 2009 Jan;7(1):13-24 9660787 - J Biol Chem. 1998 Jul 17;273(29):18242-9 9465074 - Proc Natl Acad Sci U S A. 1998 Feb 17;95(4):1669-74 18284575 - Mol Microbiol. 2008 Mar;67(6):1307-19 10322433 - Trends Biochem Sci. 1999 May;24(5):181-5 18667692 - Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10955-60 20028808 - Infect Immun. 2010 Mar;78(3):1123-34 18811729 - Mol Microbiol. 2008 Nov;70(4):908-23 15688063 - Nat Rev Mol Cell Biol. 2005 Jan;6(1):9-20 15215403 - Nucleic Acids Res. 2004 Jul 1;32(Web Server issue):W321-6 11390363 - Genes Dev. 2001 Jun 1;15(11):1435-48 18670632 - PLoS Pathog. 2008;4(8):e1000117 10352012 - J Cell Biol. 1999 May 31;145(5):933-50 17101649 - Infect Immun. 2007 Feb;75(2):592-603 9452389 - Science. 1998 Feb 6;279(5352):873-6 18363881 - Cell Microbiol. 2008 Jun;10(6):1209-20 15520000 - J Biol Chem. 2005 Jan 14;280(2):1392-400 19016782 - Cell Microbiol. 2009 Feb;11(2):261-78 18279343 - Environ Microbiol. 2008 Jun;10(6):1460-74 16267296 - J Bacteriol. 2005 Nov;187(22):7716-26 15467720 - Nat Genet. 2004 Nov;36(11):1165-73 TF Smith (ref26) 1999; 24 F Habyarimana (ref7) GM Conover (ref29) 2003; 48 ID Russell (ref15) 1999; 145 CY Chung (ref22) 1998; 12 JP Vogel (ref5) 1998; 279 M Molmeret (ref1) 2005; 71 F Habyarimana (ref9) 2008; 10 HL Ennis (ref19) 2000; 97 S Shin (ref3) 2008; 10 BA Schulman (ref14) 2000; 408 G Segal (ref4) 1998; 95 KS de Felipe (ref6) 2008; 4 B Rost (ref38) 2004; 32 C Cazalet (ref34) 2004; 36 S Mohanty (ref21) 2001; 15 RR Isberg (ref2) 2009; 7 CM West (ref23) 1997; 200 MD Petroski (ref12) 2005; 6 T Kubori (ref30) 2008; 67 Q Hu (ref18) 1997; 1351 N Kondo-Okamoto (ref16) 2006; 17 P Teng-umnuay (ref24) 1998; 273 MS Dorer (ref28) 2006; 2 AM Neves (ref17) 1991; 2 KS de Felipe (ref35) 2005; 187 M Santic (ref36) 2007; 75 S Al-Khodor (ref8) HL Ennis (ref20) 2003; 154 S Al-Khodor (ref10) 2008; 70 Y Liu (ref11) 2007; 75 B Kobe (ref25) 2001; 11 O Kerscher (ref13) 2006; 22 AR Willems (ref31) 2004; 1695 S Sonnberg (ref37) 2008; 105 SS Ivanov (ref32) 2009; 11 JC Amor (ref33) 2005; 280 E Veiga (ref27) 2005; 15 |
References_xml | – volume: 11 start-page: 261 year: 2009 ident: ref32 article-title: Modulation of ubiquitin dynamics and suppression of DALIS formation by the Legionella pneumophila Dot/Icm system. publication-title: Cell Microbiol doi: 10.1111/j.1462-5822.2008.01251.x contributor: fullname: SS Ivanov – volume: 200 start-page: 1 year: 1997 ident: ref23 article-title: The cytosolic glycoprotein FP21 of Dictyostelium discoideum is encoded by two genes resulting in a polymorphism at a single amino acid position. publication-title: Gene doi: 10.1016/S0378-1119(97)00194-7 contributor: fullname: CM West – volume: 22 start-page: 159 year: 2006 ident: ref13 article-title: Modification of proteins by ubiquitin and ubiquitin-like proteins. publication-title: Annu Rev Cell Dev Biol doi: 10.1146/annurev.cellbio.22.010605.093503 contributor: fullname: O Kerscher – volume: 2 start-page: 173 year: 1991 ident: ref17 article-title: The macronuclear polyubiquitin gene of the ciliate Tetrahymena pyriformis. publication-title: DNA Seq doi: 10.3109/10425179109039687 contributor: fullname: AM Neves – volume: 6 start-page: 9 year: 2005 ident: ref12 article-title: Function and regulation of cullin-RING ubiquitin ligases. publication-title: Nat Rev Mol Cell Biol doi: 10.1038/nrm1547 contributor: fullname: MD Petroski – volume: 10 start-page: 1209 year: 2008 ident: ref3 article-title: Host cell processes that influence the intracellular survival of Legionella pneumophila. publication-title: Cell Microbiol doi: 10.1111/j.1462-5822.2008.01145.x contributor: fullname: S Shin – volume: 15 start-page: 2 year: 2005 ident: ref27 article-title: Ubiquitination of intracellular bacteria: a new bacteria-sensing system? publication-title: Trends Cell Biol doi: 10.1016/j.tcb.2004.11.005 contributor: fullname: E Veiga – ident: ref7 article-title: Molecular characterization of the Dot/Icm-translocated AnkH and AnkJ eukaryotic-like effectors of Legionella pneumophila. contributor: fullname: F Habyarimana – volume: 408 start-page: 381 year: 2000 ident: ref14 article-title: Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex. publication-title: Nature doi: 10.1038/35042620 contributor: fullname: BA Schulman – volume: 48 start-page: 305 year: 2003 ident: ref29 article-title: The Legionella pneumophila LidA protein: a translocated substrate of the Dot/Icm system associated with maintenance of bacterial integrity. publication-title: Mol Microbiol doi: 10.1046/j.1365-2958.2003.03400.x contributor: fullname: GM Conover – volume: 75 start-page: 592 year: 2007 ident: ref11 article-title: The Legionella pneumophila effector SidJ is required for efficient recruitment of endoplasmic reticulum proteins to the bacterial phagosome. publication-title: Infect Immun doi: 10.1128/IAI.01278-06 contributor: fullname: Y Liu – volume: 75 start-page: 2903 year: 2007 ident: ref36 article-title: Host-dependent trigger of caspases and apoptosis by Legionella pneumophila. publication-title: Infect Immun doi: 10.1128/IAI.00147-07 contributor: fullname: M Santic – volume: 67 start-page: 1307 year: 2008 ident: ref30 article-title: Legionella translocates an E3 ubiquitin ligase that has multiple U-boxes with distinct functions. publication-title: Mol Microbiol doi: 10.1111/j.1365-2958.2008.06124.x contributor: fullname: T Kubori – ident: ref8 article-title: Microbial Eukaryotic-like Ankyrins: conserved structures with functional diversity to modulate host-pathogen interactions. contributor: fullname: S Al-Khodor – volume: 17 start-page: 3756 year: 2006 ident: ref16 article-title: The novel F-box protein Mfb1p regulates mitochondrial connectivity and exhibits asymmetric localization in yeast. publication-title: Mol Biol Cell doi: 10.1091/mbc.E06-02-0145 contributor: fullname: N Kondo-Okamoto – volume: 12 start-page: 3564 year: 1998 ident: ref22 article-title: A novel, putative MEK kinase controls developmental timing and spatial patterning in Dictyostelium and is regulated by ubiquitin-mediated protein degradation. publication-title: Genes Dev doi: 10.1101/gad.12.22.3564 contributor: fullname: CY Chung – volume: 105 start-page: 10955 year: 2008 ident: ref37 article-title: Poxvirus ankyrin repeat proteins are a unique class of F-box proteins that associate with cellular SCF1 ubiquitin ligase complexes. publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.0802042105 contributor: fullname: S Sonnberg – volume: 24 start-page: 181 year: 1999 ident: ref26 article-title: The WD repeat: a common architecture for diverse functions. publication-title: Trends Biochem Sci doi: 10.1016/S0968-0004(99)01384-5 contributor: fullname: TF Smith – volume: 2 start-page: e34 year: 2006 ident: ref28 article-title: RNA interference analysis of Legionella in Drosophila cells: exploitation of early secretory apparatus dynamics. publication-title: PLoS Pathog doi: 10.1371/journal.ppat.0020034 contributor: fullname: MS Dorer – volume: 279 start-page: 873 year: 1998 ident: ref5 article-title: Conjugative transfer by the virulence system of Legionella pneumophila. publication-title: Science doi: 10.1126/science.279.5352.873 contributor: fullname: JP Vogel – volume: 7 start-page: 13 year: 2009 ident: ref2 article-title: The Legionella pneumophila replication vacuole: making a cosy niche inside host cells. publication-title: Nat Rev Microbiol doi: 10.1038/nrmicro1967 contributor: fullname: RR Isberg – volume: 95 start-page: 1669 year: 1998 ident: ref4 article-title: Host cell killing and bacterial conjugation require overlapping sets of genes within a 22-kb region of the Legionella pneumophila genome. publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.95.4.1669 contributor: fullname: G Segal – volume: 36 start-page: 1165 year: 2004 ident: ref34 article-title: Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity. publication-title: Nat Genet doi: 10.1038/ng1447 contributor: fullname: C Cazalet – volume: 187 start-page: 7716 year: 2005 ident: ref35 article-title: Evidence for acquisition of Legionella type IV secretion substrates via interdomain horizontal gene transfer. publication-title: J Bacteriol doi: 10.1128/JB.187.22.7716-7726.2005 contributor: fullname: KS de Felipe – volume: 11 start-page: 725 year: 2001 ident: ref25 article-title: The leucine-rich repeat as a protein recognition motif. publication-title: Curr Opin Struct Biol doi: 10.1016/S0959-440X(01)00266-4 contributor: fullname: B Kobe – volume: 97 start-page: 3292 year: 2000 ident: ref19 article-title: Dictyostelium amoebae lacking an F-box protein form spores rather than stalk in chimeras with wild type. publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.97.7.3292 contributor: fullname: HL Ennis – volume: 15 start-page: 1435 year: 2001 ident: ref21 article-title: Regulated protein degradation controls PKA function and cell-type differentiation in Dictyostelium. publication-title: Genes Dev doi: 10.1101/gad.871101 contributor: fullname: S Mohanty – volume: 32 start-page: W321 year: 2004 ident: ref38 article-title: The PredictProtein server. publication-title: Nucleic Acids Res doi: 10.1093/nar/gkh377 contributor: fullname: B Rost – volume: 145 start-page: 933 year: 1999 ident: ref15 article-title: The unstable F-box protein p58-Ctf13 forms the structural core of the CBF3 kinetochore complex. publication-title: J Cell Biol doi: 10.1083/jcb.145.5.933 contributor: fullname: ID Russell – volume: 1351 start-page: 126 year: 1997 ident: ref18 article-title: An Acanthamoeba polyubiquitin gene and application of its promoter to the establishment of a transient transfection system. publication-title: Biochim Biophys Acta doi: 10.1016/S0167-4781(96)00185-6 contributor: fullname: Q Hu – volume: 273 start-page: 18242 year: 1998 ident: ref24 article-title: The cytoplasmic F-box binding protein SKP1 contains a novel pentasaccharide linked to hydroxyproline in Dictyostelium. publication-title: J Biol Chem doi: 10.1074/jbc.273.29.18242 contributor: fullname: P Teng-umnuay – volume: 1695 start-page: 133 year: 2004 ident: ref31 article-title: A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin. publication-title: Biochim Biophys Acta doi: 10.1016/j.bbamcr.2004.09.027 contributor: fullname: AR Willems – volume: 280 start-page: 1392 year: 2005 ident: ref33 article-title: The structure of RalF, an ADP-ribosylation factor guanine nucleotide exchange factor from Legionella pneumophila, reveals the presence of a cap over the active site. publication-title: J Biol Chem doi: 10.1074/jbc.M410820200 contributor: fullname: JC Amor – volume: 10 start-page: 1460 year: 2008 ident: ref9 article-title: Role for the Ankyrin eukaryotic-like genes of Legionella pneumophila in parasitism of protozoan hosts and human macrophages. publication-title: Environ Microbiol doi: 10.1111/j.1462-2920.2007.01560.x contributor: fullname: F Habyarimana – volume: 4 start-page: e1000117 year: 2008 ident: ref6 article-title: Legionella eukaryotic-like type IV substrates interfere with organelle trafficking. publication-title: PLoS Pathog doi: 10.1371/journal.ppat.1000117 contributor: fullname: KS de Felipe – volume: 70 start-page: 908 year: 2008 ident: ref10 article-title: A Dot/Icm-translocated ankyrin protein of Legionella pneumophila is required for intracellular proliferation within human macrophages and protozoa. publication-title: Mol Microbiol doi: 10.1111/j.1365-2958.2008.06453.x contributor: fullname: S Al-Khodor – volume: 71 start-page: 20 year: 2005 ident: ref1 article-title: Amoebae as training grounds for intracellular bacterial pathogens. publication-title: Appl Environ Microbiol doi: 10.1128/AEM.71.1.20-28.2005 contributor: fullname: M Molmeret – volume: 154 start-page: 419 year: 2003 ident: ref20 article-title: Mutation of the Dictyostelium fbxA gene affects cell-fate decisions and spatial patterning. publication-title: 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Snippet | The ability of Legionella pneumophila to proliferate within various protozoa in the aquatic environment and in macrophages indicates a remarkable evolution and... The ability of Legionella pneumophila to proliferate within various protozoa in the aquatic environment and in macrophages indicates a remarkable evolution and... The ability of Legionella pneumophila to proliferate within various protozoa in the aquatic environment and in macrophages indicates a remarkable evolution... |
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SubjectTerms | Acanthamoeba Acanthamoeba - metabolism Acanthamoeba - parasitology Animals Ankyrins - metabolism Bacterial Proteins - metabolism Bacteriology Dictyostelium - metabolism Dictyostelium - parasitology Dictyostelium discoideum Genetic aspects Humans Immune response Immunoprecipitation Legionella pneumophila Legionella pneumophila - metabolism Legionella pneumophila - pathogenicity Legionnaires disease Legionnaires' Disease - metabolism Macrophages Macrophages - metabolism Macrophages - parasitology Mice Microbiology Microbiology/Cellular Microbiology and Pathogenesis Microscopy, Confocal Molecular evolution Molecular Mimicry - immunology Physiological aspects Protein Transport - physiology Proteins Transfection Ubiquitination |
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Title | Molecular mimicry by an F-box effector of Legionella pneumophila hijacks a conserved polyubiquitination machinery within macrophages and protozoa |
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