The Legionella pneumophila IcmSW Complex Interacts with Multiple Dot/Icm Effectors to Facilitate Type IV Translocation
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{"title"=>"The Legionella pneumophila IcmSW complex interacts with multiple Dot/Icm effectors to facilitate type IV translocation", "type"=>"journal", "authors"=>[{"first_name"=>"Eric D.", "last_name"=>"Cambronne", "scopus_author_id"=>"6507159969"}, {"first_name"=>"Craig R.", "last_name"=>"Roy", "scopus_author_id"=>"36081286000"}], "year"=>2007, "source"=>"PLoS Pathogens", "identifiers"=>{"isbn"=>"1553-7374 (Electronic)\\r1553-7366 (Linking)", "pmid"=>"18069892", "doi"=>"10.1371/journal.ppat.0030188", "pui"=>"351041312", "issn"=>"15537366", "sgr"=>"37849053708", "scopus"=>"2-s2.0-37849053708"}, "id"=>"4cdc580d-29b7-3e37-ae2b-db7aef08d8d3", "abstract"=>"Many gram-negative pathogens use a type IV secretion system (T4SS) to deliver effector proteins into eukaryotic host cells. The fidelity of protein translocation depends on the efficient recognition of effector proteins by the T4SS. Legionella pneumophila delivers a large number of effector proteins into eukaryotic cells using the Dot/Icm T4SS. How the Dot/Icm system is able to recognize and control the delivery of effectors is poorly understood. Recent studies suggest that the IcmS and IcmW proteins interact to form a stable complex that facilitates translocation of effector proteins by the Dot/Icm system by an unknown mechanism. Here we demonstrate that the IcmSW complex is necessary for the productive translocation of multiple Dot/Icm effector proteins. Effector proteins that were able to bind IcmSW in vitro required icmS and icmW for efficient translocation into eukaryotic cells during L. pneumophila infection. We identified regions in the effector protein SidG involved in icmSW-dependent translocation. Although the full-length SidG protein was translocated by an icmSW-dependent mechanism, deletion of amino terminal regions in the SidG protein resulted in icmSW-independent translocation, indicating that the IcmSW complex is not contributing directly to recognition of effector proteins by the Dot/Icm system. Biochemical and genetic studies showed that the IcmSW complex interacts with a central region of the SidG protein. The IcmSW interaction resulted in a conformational change in the SidG protein as determined by differences in protease sensitivity in vitro. These data suggest that IcmSW binding to effectors could enhance effector protein delivery by mediating a conformational change that facilitates T4SS recognition of a translocation domain located in the carboxyl region of the effector protein.", "link"=>"http://www.mendeley.com/research/legionella-pneumophila-icmsw-complex-interacts-multiple-doticm-effectors-facilitate-type-iv-transloc", "reader_count"=>43, "reader_count_by_academic_status"=>{"Unspecified"=>3, "Professor > Associate Professor"=>3, "Researcher"=>15, "Student > Doctoral Student"=>4, "Student > Ph. D. Student"=>8, "Student > Postgraduate"=>2, "Student > Master"=>2, "Other"=>1, "Student > Bachelor"=>2, "Lecturer"=>1, "Professor"=>2}, "reader_count_by_user_role"=>{"Unspecified"=>3, "Professor > Associate Professor"=>3, "Researcher"=>15, "Student > Doctoral Student"=>4, "Student > Ph. D. Student"=>8, "Student > Postgraduate"=>2, "Student > Master"=>2, "Other"=>1, "Student > Bachelor"=>2, "Lecturer"=>1, "Professor"=>2}, "reader_count_by_subject_area"=>{"Unspecified"=>4, "Biochemistry, Genetics and Molecular Biology"=>4, "Agricultural and Biological Sciences"=>31, "Medicine and Dentistry"=>1, "Immunology and Microbiology"=>3}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>1}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>3}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>31}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>4}, "Unspecified"=>{"Unspecified"=>4}}, "reader_count_by_country"=>{"France"=>1}, "group_count"=>0}

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  • {"month"=>"11", "year"=>"2019", "pdf_views"=>"2", "xml_views"=>"0", "html_views"=>"4"}

Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/940990"], "description"=>"<div><p>(A) E. coli expressing H<sub>6</sub>IcmW/IcmS, and either M45-RalF or M45-SidG were lysed (T), clarified, and loaded (L) onto affinity columns, washed (W), and eluted (E). Fractions were resolved on SDS-PAGE, where H<sub>6</sub>IcmW/IcmS were detected with Coomassie staining, and RalF or SidG was detected by immunoblotting with M45-specific antisera. MW indicators for the gel are shown on the left (kDa).</p><p>(B) E. coli expressing M45-SidG alone was subjected to affinity purification as in (A). M45-SidG was detected as in (A).</p><p>(C) Lysate from E. coli expressing H<sub>6</sub>IcmW/IcmS was pre-charged onto affinity column (1), washed, and subjected to lysate from E. coli expressing M45-SidG (2) (L). Flow-through (FT) was collected and the column was washed and eluted with buffer containing the indicated concentration of imidazole. M45-SidG was detected as in (A).</p><p>(D) E. coli strains expressing H<sub>6</sub>IcmS, H<sub>6</sub>IcmW, or H<sub>6</sub>LvgA and M45-SidG or M45-RalF were subjected to affinity purification as in (B). M45-SidG or M45-RalF was detected as in (A).</p><p>(E) E. coli expressing H<sub>6</sub>IcmW/IcmS, and indicated M45-tagged SidG truncations were lysed (T), clarified (S), and loaded (L) onto affinity columns, and washed and eluted with buffer containing imidazole in the indicated concentrations. Purified M45-SidG fragments were resolved on SDS-PAGE and detected as in (A).</p><p>(F) Schematic representation of the genetic (arrows) and biochemical (hatch) contribution of IcmSW on SidG translocation. At least one IcmSW binding site resides between residues 500 and 600 of SidG [<a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.0030188#ppat-0030188-b001\" target=\"_blank\">1</a>], with additional binding sites located between residues 300 and 500 [<a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.0030188#ppat-0030188-b002\" target=\"_blank\">2</a>]. The IcmSW binding region is distinct from the C-terminal translocation domain (T).</p></div>", "links"=>[], "tags"=>["binds", "sidg", "c-terminal", "translocation"], "article_id"=>611422, "categories"=>["Microbiology", "Infectious Diseases"], "users"=>["Eric D Cambronne", "Craig R Roy"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.0030188.g005", "stats"=>{"downloads"=>0, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_IcmSW_Complex_Binds_to_a_Region_of_SidG_That_Is_Distinct_from_the_C_Terminal_Translocation_Domain_/611422", "title"=>"IcmSW Complex Binds to a Region of SidG That Is Distinct from the C-Terminal Translocation Domain", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-12-07 00:23:42"}
  • {"files"=>["https://ndownloader.figshare.com/files/940731"], "description"=>"<div><p>(A) CHO FcγRII cells were infected with wild-type (black), Δ<i>icmW</i> (dark grey), Δ<i>icmS</i> (light grey), or Δ<i>icmS</i>, Δ<i>icmW</i> (white) strains expressing Cya-SidA. Total cAMP production was determined as in <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.0030188#ppat-0030188-g001\" target=\"_blank\">Figure 1</a>.</p><p>(B) CHO FcγRII cells were infected with wild-type (black) or Δ<i>icmS</i>, Δ<i>icmW</i> (grey) strains expressing the indicated Cya hybrid proteins for 1 h. Wild-type (hatch) or Δ<i>icmS</i>, Δ<i>icmW</i> (white) indicate samples that were conditioned with cytochalasin D prior to infection. Total cAMP production induced by translocation of the hybrid was determined as in (<a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.0030188#ppat-0030188-g001\" target=\"_blank\">Figure 1</a>).</p><p>(C) Immunoblots of whole-cell bacterial extracts expressing indicated Cya hybrid proteins from wild-type (WT) or Δi<i>cmS</i>, Δ<i>icmW</i> (Δ) probed with monoclonal antibody specific to the M45 epitope. Immunoblots for chloramphenicol acetyltransferase (Cat) are included as a load control.</p><p>(D) CHO FcγRII cells were infected with wild-type (black) or Δ<i>icmS</i>, Δ<i>icmW</i> (grey) L. pneumophila strains expressing Cya-SidG. Bacteria (3 × 10<sup>6</sup>; MOI = 30) were added to each well (input line) and subjected to the conditions indicated. +/− Cyto D indicates the addition of cytochalasin D (10 μM) 30 min prior to and during infection. +/− Gent indicates the addition of gentamycin (10 μM) 15 min post-infection. After 1 h of infection, tissue culture cells were washed and osmotically lysed. Lysates were serially diluted, plated, and incubated to determine total colony-forming units (CFU) from each condition. Bars represent average values ± SD of experiments performed in triplicate.</p><p>(E) Graphical representation of the average translocation efficiency of the <i>icmSW</i>-dependent substrates SidA, SidB, SidC, SidD, SidE, SidG, and SidH. Translocation of each construct in wild-type is considered 100%. The average % defect is plotted for the Δ<i>icmS</i>, Δ<i>icmW</i>, and Δ<i>icmS</i>, Δ<i>icmW</i> strains ± SD of translocation assays performed in triplicate. <i>p</i>-Values from Student's <i>t</i>-test are indicated as comparisons between strains.</p></div>", "links"=>[], "tags"=>["defects", "observed"], "article_id"=>611162, "categories"=>["Microbiology", "Infectious Diseases"], "users"=>["Eric D Cambronne", "Craig R Roy"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.0030188.g002", "stats"=>{"downloads"=>1, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Translocation_Defects_Observed_for_the_L_pneumophila_916_icmS_icmW_Double_Mutant_/611162", "title"=>"Translocation Defects Observed for the L. pneumophila Δ<i>icmS</i>, Δ<i>icmW</i> Double Mutant", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-12-07 00:19:22"}
  • {"files"=>["https://ndownloader.figshare.com/files/941202"], "description"=>"<div><p>(A) CHO FcγRII cells were infected with wild-type (black), Δ<i>dotA</i> (dark grey), or Δ<i>icmS</i>, Δ<i>icmW</i> (light grey) L. pneumophila strains expressing the indicated Cya-SidG proteins for 1 h. Cultures that were grown in the presence of 1 mM IPTG prior to and during infection are indicated (Cya-SidG<sup>++</sup>). Total cAMP production induced by translocation of the hybrid was determined as in <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.0030188#ppat-0030188-g001\" target=\"_blank\">Figure 1</a>.</p><p>(B) Immunoblots of whole-cell bacterial extracts expressing Cya-SidG cultured in the absence or presence of 1 mM IPTG (Cya-SidG<sup>++</sup>). Proteins from wild-type (WT) or Δ<i>icmS</i>, Δ<i>icmW</i> (SW) were probed with monoclonal antibody specific to the M45 epitope. Immunoblots for chloramphenicol acetyltransferase (Cat) are included as a load control.</p></div>", "links"=>[], "tags"=>["sidg", "bypass"], "article_id"=>611624, "categories"=>["Microbiology", "Infectious Diseases"], "users"=>["Eric D Cambronne", "Craig R Roy"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.0030188.g007", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Overproduction_of_SidG_Can_Bypass_the_icmSW_Requirement_/611624", "title"=>"Overproduction of SidG Can Bypass the <i>icmSW</i> Requirement", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-12-07 00:27:04"}
  • {"files"=>["https://ndownloader.figshare.com/files/941373"], "description"=>"<div><p>(A) Schematic representation of the SidG polypeptide, with the IcmSW binding domain shown (hatch) as well as the indicated C-terminal domain (876–965) used for generation of polyclonal antisera. Full-length SidG was detected at equivalent levels from wild-type (WT) or Δ<i>icmS</i>, Δ<i>icmW</i> mutant L. pneumophila (SW) and was not detected in the <i>sidG</i> deletion strain (ΔG).</p><p>(B) Recombinant RalF or SidG were co-expressed in the absence (vector) or presence of the IcmSW complex (H<sub>6</sub>IcmW,IcmS), and subjected to lysis and clarification. Aliquots of soluble whole-cell lysates were subjected to the indicated concentrations of trypsin for 1 h. Samples were subjected to SDS-PAGE and immunoblotting, where proteolytic fragments of RalF (RalF−) or SidG (SidG−) were detected with specific antisera raised against the indicated polypeptides. The black arrow indicates predominant cleavage product.</p><p>(C) Lysates containing SidG were processed as in (B), except that trypsin was diluted 1,000-fold. Proteolytic cleavage fragments (white arrows) emerge in the absence of IcmSW in the molecular size range of 50–60 kDa as indicated by the asterisk.</p><p>(D) Proteolytic time course experiment performed at indicated concentration (20 ng) on SidG-containing lysates. Immunoblots show differential cleavage products (arrows) in the 50–60 kDa molecular size range (*).</p></div>", "links"=>[], "tags"=>["binding", "sidg", "conformational", "effector"], "article_id"=>611797, "categories"=>["Microbiology", "Infectious Diseases"], "users"=>["Eric D Cambronne", "Craig R Roy"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.0030188.g009", "stats"=>{"downloads"=>0, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_IcmSW_Binding_to_SidG_Promotes_Conformational_Changes_in_the_Effector_Protein_/611797", "title"=>"IcmSW Binding to SidG Promotes Conformational Changes in the Effector Protein", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-12-07 00:29:57"}
  • {"files"=>["https://ndownloader.figshare.com/files/941274"], "description"=>"<div><p>(A) CHO FcγRII cells were infected with wild-type (black), Δ<i>dotA</i> (dark grey), or Δ<i>icmS</i>, Δ<i>icmW</i> (light grey) strains expressing the indicated Cya hybrid proteins. Total cAMP production induced by translocation of the hybrid was determined as in (<a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.0030188#ppat-0030188-g001\" target=\"_blank\">Figure 1</a>). % values represent translocation efficiency as a measure of (Δ<i>icmS</i>, Δ<i>icmW</i>) / wild-type.</p><p>(B) Immunoblots of whole-cell bacterial extracts expressing Cya-SidG<i><sup>FLAG</sup></i> or Cya-RalF<i><sup>FLAG</sup></i> proteins from wild-type (WT) or Δ<i>icmS</i>, Δ<i>icmW</i> (Δ) probed with monoclonal antibodies specific to the M45 or FLAG epitopes. Immunoblots for chloramphenicol acetyltransferase (Cat) are included as a load control.</p><p>(C) Immunoblots of whole-cell bacterial extracts expressing SidG<i><sup>FLAG</sup></i> from wild-type (WT) or Δ<i>icmS</i>, Δ<i>icmW</i> (SW) probed with monoclonal antibody specific to the FLAG epitope.</p><p>(D) SidG<i><sup>FLAG</sup></i> was expressed in wild-type or Δ<i>icmS</i>, Δ<i>icmW L. pneumophila</i> strains to stationary phase. Cultures were harvested, lysed in the absence of protease inhibitors, and clarified. Lysates were subjected to serial dilutions that were mixed with sample buffer and analyzed by SDS-PAGE and immunoblotting with monoclonal antisera specific for the FLAG epitope.</p></div>", "links"=>[], "tags"=>["c-terminal", "epitope", "alters", "sidg"], "article_id"=>611696, "categories"=>["Microbiology", "Infectious Diseases"], "users"=>["Eric D Cambronne", "Craig R Roy"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.0030188.g008", "stats"=>{"downloads"=>0, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_A_C_Terminal_FLAG_Epitope_Alters_the_Requirement_for_icmSW_in_SidG_Translocation_/611696", "title"=>"A C-Terminal FLAG Epitope Alters the Requirement for <i>icmSW</i> in SidG Translocation", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-12-07 00:28:16"}
  • {"files"=>["https://ndownloader.figshare.com/files/940850"], "description"=>"<div><p>(A) Schematic representation of the 965-aa SidG protein, which contains an extensive coiled-coil region (grey) as well as two hydrophobic segments (black). The identified translocation signal is depicted (T).</p><p>(B and C) CHO FcγRII cells were infected with wild-type (black) or Δ<i>dotA</i> (dark grey) strains expressing the indicated Cya-SidG hybrid proteins for 1 h. Total cAMP production induced by translocation of the hybrid was determined as in <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.0030188#ppat-0030188-g001\" target=\"_blank\">Figure 1</a>.</p></div>", "links"=>[], "tags"=>["contains", "c-terminal", "translocation"], "article_id"=>611278, "categories"=>["Microbiology", "Infectious Diseases"], "users"=>["Eric D Cambronne", "Craig R Roy"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.0030188.g003", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_SidG_Contains_a_C_Terminal_Translocation_Signal_/611278", "title"=>"SidG Contains a C-Terminal Translocation Signal", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-12-07 00:21:18"}
  • {"files"=>["https://ndownloader.figshare.com/files/940663"], "description"=>"<div><p>(A) CHO FcγRII cells were left uninfected (hatch), or infected with wild-type (black), Δ<i>icmS</i> (light grey), or Δ<i>icmW</i> (dark grey) L. pneumophila strains expressing the indicated Cya hybrid proteins. After 1 h of infection, tissue culture cells were lysed and cAMP was extracted from the sample. Total cAMP production induced by translocation of the hybrid was quantified using an enzyme-immunoassay system, indicated as fmol. Results represent average values ± SD of experiments performed in triplicate.</p><p>(B) Immunoblots of whole-cell bacterial extracts expressing indicated Cya hybrid proteins from wild-type (WT), Δ<i>dotA</i> (A), Δ<i>icmS</i> (S), and Δ<i>icmW</i> (W) probed with monoclonal antibody specific to the M45 epitope.</p></div>", "links"=>[], "tags"=>["icmsw", "translocation", "effector"], "article_id"=>611100, "categories"=>["Microbiology", "Infectious Diseases"], "users"=>["Eric D Cambronne", "Craig R Roy"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.0030188.g001", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_IcmSW_Complex_Is_Necessary_for_the_Translocation_of_Multiple_Effector_Proteins_/611100", "title"=>"The IcmSW Complex Is Necessary for the Translocation of Multiple Effector Proteins", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-12-07 00:18:20"}
  • {"files"=>["https://ndownloader.figshare.com/files/940926"], "description"=>"<div><p>(A) CHO FcγRII cells were infected with wild-type (black), Δ<i>dotA</i> (dark grey), or Δ<i>icmS</i>, Δ<i>icmW</i> (light grey) strains expressing indicated Cya-SidG hybrid proteins for 1 h. Total cAMP production induced by translocation of the hybrid was determined as in <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.0030188#ppat-0030188-g001\" target=\"_blank\">Figure 1</a>.</p><p>(B) CHO FcγRII cells were infected with wild-type or Δ<i>icmS</i>, Δ<i>icmW</i> strains expressing the indicated Cya-SidG hybrid proteins for 1 h. Total cAMP production induced by translocation of the hybrid was determined for each strain. % values represent translocation efficiency as a measure of (Δ<i>icmS</i>, Δ<i>icmW</i>) / wild-type for the indicated Cya-SidG hybrid proteins. + indicates that cAMP production induced by translocation of the hybrid in Δ<i>icmS</i>, Δ<i>icmW</i> exceeded levels produced in wild-type.</p></div>", "links"=>[], "tags"=>["c-terminal", "translocation", "sidg", "supports"], "article_id"=>611353, "categories"=>["Microbiology", "Infectious Diseases"], "users"=>["Eric D Cambronne", "Craig R Roy"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.0030188.g004", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_C_Terminal_Translocation_Signal_of_SidG_Supports_icmSW_Independent_Translocation_/611353", "title"=>"The C-Terminal Translocation Signal of SidG Supports <i>icmSW</i>-Independent Translocation", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-12-07 00:22:33"}
  • {"files"=>["https://ndownloader.figshare.com/files/941091"], "description"=>"<div><p>(A) Immunoblots of whole-cell bacterial extracts expressing M45-SidG or M45-RalF proteins from wild-type (WT) or Δ<i>icmS</i>, Δ<i>icmW</i> (SW) probed with monoclonal antibody specific to the M45 epitope. Immunoblots for chloramphenicol acetyltransferase (Cat) are included as a load control.</p><p>(B) Aliquots containing total protein from stationary phase wild-type or Δ<i>icmS</i>, Δ<i>icmW L. pneumophila</i> strains were precipitated (−). Cultures were harvested, resuspended in media containing kanamycin, and allowed to incubate at 37 °C for times indicated. Aliquots were mixed in sample buffer, resolved on SDS-PAGE, and detected with immunoblotting.</p><p>(C) Wild-type or Δ<i>icmS</i>, Δ<i>icmW</i> mutant L. pneumophila expressing M45-RalF was cultured to stationary phase, harvested, lysed, and clarified (T). Ultracentrifugation separated a soluble (S) fraction from insoluble material. Inner membrane protein extraction with TritonX-100 (X) and subsequent ultracentrifugation separated this population from insoluble material (I). Protein contained in each fraction was detected with SDS-PAGE and immunoblotting. Immunoblots for (Cat) are included as a soluble protein control.</p><p>(D) Wild-type or Δ<i>icmS</i>, Δ<i>icmW</i> mutant L. pneumophila expressing M45-SidG or indicated (*) SidG truncation proteins were cultured and subjected to sub-cellular fractionation as in (C). Protein contained in each fraction was detected with SDS-PAGE and immunoblotting. Immunoblots for (Cat) are included as a soluble protein control.</p></div>", "links"=>[], "tags"=>["sub-cellular", "localization"], "article_id"=>611519, "categories"=>["Microbiology", "Infectious Diseases"], "users"=>["Eric D Cambronne", "Craig R Roy"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.0030188.g006", "stats"=>{"downloads"=>4, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_IcmSW_Complex_Does_Not_Influence_the_Stability_Solubility_or_Sub_Cellular_Localization_of_SidG_/611519", "title"=>"IcmSW Complex Does Not Influence the Stability, Solubility, or Sub-Cellular Localization of SidG", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-12-07 00:25:19"}
  • {"files"=>["https://ndownloader.figshare.com/files/463339", "https://ndownloader.figshare.com/files/463376", "https://ndownloader.figshare.com/files/463414", "https://ndownloader.figshare.com/files/463442", "https://ndownloader.figshare.com/files/463464", "https://ndownloader.figshare.com/files/463489", "https://ndownloader.figshare.com/files/463535"], "description"=>"<div><p>Many Gram-negative pathogens use a type IV secretion system (T4SS) to deliver effector proteins into eukaryotic host cells. The fidelity of protein translocation depends on the efficient recognition of effector proteins by the T4SS. Legionella pneumophila delivers a large number of effector proteins into eukaryotic cells using the Dot/Icm T4SS. How the Dot/Icm system is able to recognize and control the delivery of effectors is poorly understood. Recent studies suggest that the IcmS and IcmW proteins interact to form a stable complex that facilitates translocation of effector proteins by the Dot/Icm system by an unknown mechanism. Here we demonstrate that the IcmSW complex is necessary for the productive translocation of multiple Dot/Icm effector proteins. Effector proteins that were able to bind IcmSW in vitro required <em>icmS</em> and <em>icmW</em> for efficient translocation into eukaryotic cells during L. pneumophila infection. We identified regions in the effector protein SidG involved in <em>icmSW</em>-dependent translocation. Although the full-length SidG protein was translocated by an <em>icmSW</em>-dependent mechanism, deletion of amino terminal regions in the SidG protein resulted in <em>icmSW</em>-independent translocation, indicating that the IcmSW complex is not contributing directly to recognition of effector proteins by the Dot/Icm system. Biochemical and genetic studies showed that the IcmSW complex interacts with a central region of the SidG protein. The IcmSW interaction resulted in a conformational change in the SidG protein as determined by differences in protease sensitivity in vitro. These data suggest that IcmSW binding to effectors could enhance effector protein delivery by mediating a conformational change that facilitates T4SS recognition of a translocation domain located in the carboxyl region of the effector protein.</p></div>", "links"=>[], "tags"=>["icmsw", "interacts", "effectors", "iv", "translocation"], "article_id"=>151321, "categories"=>["Cancer", "Microbiology"], "users"=>["Eric D Cambronne", "Craig R Roy"], "doi"=>["https://dx.doi.org/10.1371/journal.ppat.0030188.sg001", "https://dx.doi.org/10.1371/journal.ppat.0030188.sg002", "https://dx.doi.org/10.1371/journal.ppat.0030188.sg003", "https://dx.doi.org/10.1371/journal.ppat.0030188.sg004", "https://dx.doi.org/10.1371/journal.ppat.0030188.sg005", "https://dx.doi.org/10.1371/journal.ppat.0030188.sd001", "https://dx.doi.org/10.1371/journal.ppat.0030188.st001"], "stats"=>{"downloads"=>30, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/The_Legionella_pneumophila_IcmSW_Complex_Interacts_with_Multiple_Dot_Icm_Effectors_to_Facilitate_Type_IV_Translocation/151321", "title"=>"The Legionella pneumophila IcmSW Complex Interacts with Multiple Dot/Icm Effectors to Facilitate Type IV Translocation", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2007-12-07 00:22:01"}

PMC Usage Stats | Further Information

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  • {"scanned-page-browse"=>"0", "month"=>"4", "cited-by"=>"0", "abstract"=>"0", "full-text"=>"9", "unique-ip"=>"8", "pdf"=>"8", "year"=>"2010", "figure"=>"0", "scanned-summary"=>"0", "supp-data"=>"0"}
  • {"month"=>"5", "scanned-page-browse"=>"0", "cited-by"=>"0", "abstract"=>"2", "full-text"=>"4", "year"=>"2010", "pdf"=>"1", "unique-ip"=>"7", "figure"=>"0", "scanned-summary"=>"0", "supp-data"=>"0"}
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  • {"month"=>"7", "scanned-page-browse"=>"0", "cited-by"=>"0", "abstract"=>"0", "full-text"=>"12", "year"=>"2010", "pdf"=>"6", "unique-ip"=>"11", "figure"=>"0", "scanned-summary"=>"0", "supp-data"=>"3"}
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Relative Metric

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