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The Chlamydia trachomatis effector CT226 directly engages LRRFIP1 to recruit a multiprotein complex that limits inclusion size and progeny production.

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Τίτλος: The Chlamydia trachomatis effector CT226 directly engages LRRFIP1 to recruit a multiprotein complex that limits inclusion size and progeny production.
Συγγραφείς: Elwell CA; University of California San Francisco, San Francisco, California, USA., Diallo A; University of California San Francisco, San Francisco, California, USA., Sixt BS; Duke University Medical Center, Durham, North Carolina, USA., Sherry J; University of California San Francisco, San Francisco, California, USA., Pha K; University of California San Francisco, San Francisco, California, USA., Valdivia RH; Duke University Medical Center, Durham, North Carolina, USA., Rosenberg O; University of California San Francisco, San Francisco, California, USA., Verba K; University of California San Francisco, San Francisco, California, USA., Engel J; University of California San Francisco, San Francisco, California, USA.
Πηγή: MBio [mBio] 2026 Oct 14; Vol. 17 (10), pp. e0195326. Date of Electronic Publication: 2026 Sep 17.
Τύπος έκδοσης: Journal Article
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: American Society for Microbiology Country of Publication: United States NLM ID: 101519231 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 2150-7511 (Electronic) NLM ISO Abbreviation: mBio Subsets: MEDLINE
Imprint Name(s): Original Publication: Washington, D.C. : American Society for Microbiology
Ιατρικοί όροι (MeSH): Chlamydia trachomatis*/genetics , Chlamydia trachomatis*/metabolism , Chlamydia trachomatis*/growth & development , Bacterial Proteins*/metabolism , Bacterial Proteins*/genetics , Inclusion Bodies*/microbiology , Inclusion Bodies*/metabolism , Multiprotein Complexes*/metabolism , Membrane Proteins*/metabolism , Membrane Proteins*/genetics , Host-Pathogen Interactions*, Chlamydia Infections/microbiology ; Humans ; Protein Binding ; HeLa Cells
Περίληψη: Chlamydia species secrete a unique class of effector proteins termed inclusion membrane proteins (Incs) that are translocated into the inclusion membrane and reprogram host cell processes to support intracellular growth. Using affinity purification-mass spectrometry, we previously identified an interaction between the early expressed Inc CT226 and a human multiprotein complex comprising leucine-rich repeat Flightless-I-interacting protein 1 (LRRFIP1), LRRFIP2, Flightless-I (FLII), and tropomodulin 3 (TMOD3). Here, we define the molecular basis and functional consequences of this interaction during Chlamydia trachomatis infection. We show that CT226 is both necessary and sufficient to recruit the LRRFIP1/2:FLII:TMOD3 (LFT) complex to the inclusion membrane. In vitro reconstitution with purified proteins demonstrates that the predicted coiled-coil region of CT226 directly binds the N-terminal helix of LRRFIP1. Using in silico structural modeling with AlphaFold-Multimer coupled with mutational validation, we identify key residues that mediate an electrostatic CT226:LRRFIP1 interaction required for LFT recruitment to the inclusion. Unexpectedly, genetic disruption of CT226 or its interaction with the LFT complex results in modest increases in inclusion size and recovery of infectious progeny late in infection, demonstrating that the CT226:LFT interaction modulates C. trachomatis developmental progression. Together, these findings establish the molecular basis of CT226-mediated recruitment of the LFT complex to the inclusion membrane and uncover a previously unrecognized role for this effector-host interaction at late timepoints of the C. trachomatis intracellular developmental cycle.IMPORTANCEChlamydia trachomatis is a major cause of sexually transmitted infections and blindness worldwide. This bacterium survives by replicating inside host cells within a membrane-bound compartment, where it deploys specialized proteins to manipulate host processes. These proteins, known as inclusion membrane proteins (Incs), help organize the host-pathogen interface, but the molecular mechanisms by which many Incs engage host factors remain poorly understood. Here, we show that the Inc protein CT226 recruits a host multiprotein complex to the bacterial compartment by directly binding one of its components. Using structural modeling and targeted mutations, we define the molecular interface required for this interaction. Disruption of CT226 or its ability to engage this host complex results in modest increases in inclusion size and production of infectious progeny, suggesting a role for the CT226:host interaction in regulating Chlamydia intracellular development. These findings reveal how a bacterial effector can engage a host protein complex to influence the outcome of infection.
Competing Interests: The authors declare no conflict of interest.
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Nature. 2011 Dec 21;481(7381):365-70. (PMID: 22190034)
PLoS Pathog. 2015 Jun 04;11(6):e1004883. (PMID: 26042774)
Cell Rep. 2024 Aug 27;43(8):114624. (PMID: 39154341)
Front Immunol. 2023 Jun 28;14:1209879. (PMID: 37449211)
Blood. 2010 Nov 25;116(22):4646-56. (PMID: 20833976)
Infect Immun. 2021 Jun 16;89(7):e0009421. (PMID: 33875478)
PLoS One. 2019 Nov 7;14(11):e0224324. (PMID: 31697687)
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Cells. 2019 Jan 31;8(2):. (PMID: 30709060)
Microb Cell. 2019 Aug 21;6(9):414-449. (PMID: 31528632)
Proc Natl Acad Sci U S A. 2023 May 9;120(19):e2213696120. (PMID: 37126682)
PLoS Pathog. 2014 Jul 31;10(7):e1004286. (PMID: 25080348)
J Infect Dis. 2010 Jun 15;201 Suppl 2:S114-25. (PMID: 20524234)
Cell Host Microbe. 2015 Jul 8;18(1):109-21. (PMID: 26118995)
Nucleic Acids Res. 2021 Jan 8;49(D1):D458-D460. (PMID: 33104802)
Proteins. 2011 Mar;79(3):898-915. (PMID: 21287621)
Nat Rev Microbiol. 2016 Jun;14(6):385-400. (PMID: 27108705)
Genomics. 1999 Jun 1;58(2):146-57. (PMID: 10366446)
Front Cell Dev Biol. 2020 Nov 24;8:603508. (PMID: 33330501)
Proc Natl Acad Sci U S A. 2003 Jul 8;100(14):8478-83. (PMID: 12815105)
Infect Immun. 2015 Dec;83(12):4710-8. (PMID: 26416906)
PLoS One. 2013;8(2):e57090. (PMID: 23441233)
Nat Methods. 2022 Jun;19(6):679-682. (PMID: 35637307)
Infect Immun. 2002 Jun;70(6):2741-51. (PMID: 12010958)
Nucleic Acids Res. 2022 Jul 5;50(W1):W276-W279. (PMID: 35412617)
Microbes Infect. 2002 Mar;4(3):333-40. (PMID: 11909744)
mSphere. 2024 Nov 21;9(11):e0047324. (PMID: 39404459)
J Bacteriol. 2004 Nov;186(21):7344-52. (PMID: 15489446)
Cell Host Microbe. 2017 Jan 11;21(1):113-121. (PMID: 28041929)
Mol Cell. 2018 Aug 16;71(4):637-648.e5. (PMID: 30118682)
Virulence. 2025 Dec;16(1):2503423. (PMID: 40353442)
PLoS Pathog. 2011 Feb;7(2):e1001289. (PMID: 21390206)
PLoS One. 2013 Dec 31;8(12):e83989. (PMID: 24391860)
J Bacteriol. 2014 Apr;196(7):1325-34. (PMID: 24443531)
Mol Cell. 2015 Jan 22;57(2):329-340. (PMID: 25616068)
FEMS Microbiol Rev. 2016 Nov 1;40(6):875-893. (PMID: 28201690)
Nat Methods. 2011 Jun 26;8(8):659-61. (PMID: 21706014)
Infect Immun. 2019 Oct 18;87(11):. (PMID: 31405957)
Microbes Infect. 2018 Aug - Sep;20(7-8):424-431. (PMID: 29248634)
J Struct Biol. 2013 Jan;181(1):82-8. (PMID: 23099021)
Cell Microbiol. 2000 Feb;2(1):35-47. (PMID: 11207561)
PLoS Pathog. 2011 Sep;7(9):e1002258. (PMID: 21966270)
Trends Microbiol. 2016 Jun;24(6):450-462. (PMID: 26924068)
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Protein Sci. 2018 Jan;27(1):14-25. (PMID: 28710774)
PLoS Pathog. 2019 Apr 3;15(4):e1007698. (PMID: 30943267)
Grant Information: R56AI152526 National Institute of Allergy and Infectious Diseases; R01AI122747 National Institute of Allergy and Infectious Diseases
Contributed Indexing: Keywords: Chlamydia trachomatis; Flightless; LRRFIP1; LRRFIP2; TMOD; alphafold; host–pathogen interactions; inclusion membrane protein; intracellular bacteria; microbial cell biology; vacuolar bacteria
Substance Nomenclature: 0 (Bacterial Proteins)
0 (Multiprotein Complexes)
0 (Membrane Proteins)
Entry Date(s): Date Created: 20260917 Date Completed: 20261014 Latest Revision: 20261029
Update Code: 20261029
PubMed Central ID: PMC13712786
DOI: 10.1128/mbio.01953-26
PMID: 42752221
Βάση Δεδομένων: MEDLINE
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  Data: The Chlamydia trachomatis effector CT226 directly engages LRRFIP1 to recruit a multiprotein complex that limits inclusion size and progeny production.
– Name: Author
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  Data: <searchLink fieldCode="AU" term="%22Elwell+CA%22">Elwell CA</searchLink>; University of California San Francisco, San Francisco, California, USA.<br /><searchLink fieldCode="AU" term="%22Diallo+A%22">Diallo A</searchLink>; University of California San Francisco, San Francisco, California, USA.<br /><searchLink fieldCode="AU" term="%22Sixt+BS%22">Sixt BS</searchLink>; Duke University Medical Center, Durham, North Carolina, USA.<br /><searchLink fieldCode="AU" term="%22Sherry+J%22">Sherry J</searchLink>; University of California San Francisco, San Francisco, California, USA.<br /><searchLink fieldCode="AU" term="%22Pha+K%22">Pha K</searchLink>; University of California San Francisco, San Francisco, California, USA.<br /><searchLink fieldCode="AU" term="%22Valdivia+RH%22">Valdivia RH</searchLink>; Duke University Medical Center, Durham, North Carolina, USA.<br /><searchLink fieldCode="AU" term="%22Rosenberg+O%22">Rosenberg O</searchLink>; University of California San Francisco, San Francisco, California, USA.<br /><searchLink fieldCode="AU" term="%22Verba+K%22">Verba K</searchLink>; University of California San Francisco, San Francisco, California, USA.<br /><searchLink fieldCode="AU" term="%22Engel+J%22">Engel J</searchLink>; University of California San Francisco, San Francisco, California, USA.
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  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22American+Society+for+Microbiology%22">American Society for Microbiology </searchLink><i>Country of Publication: </i>United States <i>NLM ID: </i>101519231 <i>Publication Model: </i>Print-Electronic <i>Cited Medium: </i>Internet <i>ISSN: </i>2150-7511 (Electronic) <i>NLM ISO Abbreviation: </i>mBio <i>Subsets: </i>MEDLINE
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  Data: <i>Original Publication</i>: Washington, D.C. : American Society for Microbiology
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  Data: <searchLink fieldCode="MM" term="%22Chlamydia+trachomatis%22">Chlamydia trachomatis*</searchLink>/<searchLink fieldCode="MM" term="%22Chlamydia+trachomatis+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Chlamydia+trachomatis%22">Chlamydia trachomatis*</searchLink>/<searchLink fieldCode="MM" term="%22Chlamydia+trachomatis+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Chlamydia+trachomatis%22">Chlamydia trachomatis*</searchLink>/<searchLink fieldCode="MM" term="%22Chlamydia+trachomatis+growth+%26+development%22">growth & development</searchLink> <br /><searchLink fieldCode="MM" term="%22Bacterial+Proteins%22">Bacterial Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Bacterial+Proteins+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Bacterial+Proteins%22">Bacterial Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Bacterial+Proteins+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Inclusion+Bodies%22">Inclusion Bodies*</searchLink>/<searchLink fieldCode="MM" term="%22Inclusion+Bodies+microbiology%22">microbiology</searchLink> <br /><searchLink fieldCode="MM" term="%22Inclusion+Bodies%22">Inclusion Bodies*</searchLink>/<searchLink fieldCode="MM" term="%22Inclusion+Bodies+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Multiprotein+Complexes%22">Multiprotein Complexes*</searchLink>/<searchLink fieldCode="MM" term="%22Multiprotein+Complexes+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Membrane+Proteins%22">Membrane Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Membrane+Proteins+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Membrane+Proteins%22">Membrane Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Membrane+Proteins+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Host-Pathogen+Interactions%22">Host-Pathogen Interactions*</searchLink><br /><searchLink fieldCode="MH" term="%22Chlamydia+Infections%22">Chlamydia Infections</searchLink>/<searchLink fieldCode="MH" term="%22Chlamydia+Infections+microbiology%22">microbiology</searchLink> ; <searchLink fieldCode="MH" term="%22Humans%22">Humans</searchLink> ; <searchLink fieldCode="MH" term="%22Protein+Binding%22">Protein Binding</searchLink> ; <searchLink fieldCode="MH" term="%22HeLa+Cells%22">HeLa Cells</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Chlamydia species secrete a unique class of effector proteins termed inclusion membrane proteins (Incs) that are translocated into the inclusion membrane and reprogram host cell processes to support intracellular growth. Using affinity purification-mass spectrometry, we previously identified an interaction between the early expressed Inc CT226 and a human multiprotein complex comprising leucine-rich repeat Flightless-I-interacting protein 1 (LRRFIP1), LRRFIP2, Flightless-I (FLII), and tropomodulin 3 (TMOD3). Here, we define the molecular basis and functional consequences of this interaction during Chlamydia trachomatis infection. We show that CT226 is both necessary and sufficient to recruit the LRRFIP1/2:FLII:TMOD3 (LFT) complex to the inclusion membrane. In vitro reconstitution with purified proteins demonstrates that the predicted coiled-coil region of CT226 directly binds the N-terminal helix of LRRFIP1. Using in silico structural modeling with AlphaFold-Multimer coupled with mutational validation, we identify key residues that mediate an electrostatic CT226:LRRFIP1 interaction required for LFT recruitment to the inclusion. Unexpectedly, genetic disruption of CT226 or its interaction with the LFT complex results in modest increases in inclusion size and recovery of infectious progeny late in infection, demonstrating that the CT226:LFT interaction modulates C. trachomatis developmental progression. Together, these findings establish the molecular basis of CT226-mediated recruitment of the LFT complex to the inclusion membrane and uncover a previously unrecognized role for this effector-host interaction at late timepoints of the C. trachomatis intracellular developmental cycle.IMPORTANCEChlamydia trachomatis is a major cause of sexually transmitted infections and blindness worldwide. This bacterium survives by replicating inside host cells within a membrane-bound compartment, where it deploys specialized proteins to manipulate host processes. These proteins, known as inclusion membrane proteins (Incs), help organize the host-pathogen interface, but the molecular mechanisms by which many Incs engage host factors remain poorly understood. Here, we show that the Inc protein CT226 recruits a host multiprotein complex to the bacterial compartment by directly binding one of its components. Using structural modeling and targeted mutations, we define the molecular interface required for this interaction. Disruption of CT226 or its ability to engage this host complex results in modest increases in inclusion size and production of infectious progeny, suggesting a role for the CT226:host interaction in regulating Chlamydia intracellular development. These findings reveal how a bacterial effector can engage a host protein complex to influence the outcome of infection.
– Name: Abstract
  Label: Competing Interests
  Group: Ab
  Data: The authors declare no conflict of interest.
– Name: Ref
  Label: References
  Group: RefInfo
  Data: Biophys Rev. 2018 Dec;10(6):1605-1615. (PMID: <searchLink fieldCode="PM" term="%2230430457%22">30430457)</searchLink><br />Nature. 2011 Dec 21;481(7381):365-70. (PMID: <searchLink fieldCode="PM" term="%2222190034%22">22190034)</searchLink><br />PLoS Pathog. 2015 Jun 04;11(6):e1004883. (PMID: <searchLink fieldCode="PM" term="%2226042774%22">26042774)</searchLink><br />Cell Rep. 2024 Aug 27;43(8):114624. (PMID: <searchLink fieldCode="PM" term="%2239154341%22">39154341)</searchLink><br />Front Immunol. 2023 Jun 28;14:1209879. (PMID: <searchLink fieldCode="PM" term="%2237449211%22">37449211)</searchLink><br />Blood. 2010 Nov 25;116(22):4646-56. (PMID: <searchLink fieldCode="PM" term="%2220833976%22">20833976)</searchLink><br />Infect Immun. 2021 Jun 16;89(7):e0009421. (PMID: <searchLink fieldCode="PM" term="%2233875478%22">33875478)</searchLink><br />PLoS One. 2019 Nov 7;14(11):e0224324. (PMID: <searchLink fieldCode="PM" term="%2231697687%22">31697687)</searchLink><br />Front Cell Infect Microbiol. 2023 May 17;13:1208302. (PMID: <searchLink fieldCode="PM" term="%2237265500%22">37265500)</searchLink><br />Cells. 2019 Jan 31;8(2):. (PMID: <searchLink fieldCode="PM" term="%2230709060%22">30709060)</searchLink><br />Microb Cell. 2019 Aug 21;6(9):414-449. (PMID: <searchLink fieldCode="PM" term="%2231528632%22">31528632)</searchLink><br />Proc Natl Acad Sci U S A. 2023 May 9;120(19):e2213696120. (PMID: <searchLink fieldCode="PM" term="%2237126682%22">37126682)</searchLink><br />PLoS Pathog. 2014 Jul 31;10(7):e1004286. (PMID: <searchLink fieldCode="PM" term="%2225080348%22">25080348)</searchLink><br />J Infect Dis. 2010 Jun 15;201 Suppl 2:S114-25. (PMID: <searchLink fieldCode="PM" term="%2220524234%22">20524234)</searchLink><br />Cell Host Microbe. 2015 Jul 8;18(1):109-21. (PMID: <searchLink fieldCode="PM" term="%2226118995%22">26118995)</searchLink><br />Nucleic Acids Res. 2021 Jan 8;49(D1):D458-D460. (PMID: <searchLink fieldCode="PM" term="%2233104802%22">33104802)</searchLink><br />Proteins. 2011 Mar;79(3):898-915. (PMID: <searchLink fieldCode="PM" term="%2221287621%22">21287621)</searchLink><br />Nat Rev Microbiol. 2016 Jun;14(6):385-400. (PMID: <searchLink fieldCode="PM" term="%2227108705%22">27108705)</searchLink><br />Genomics. 1999 Jun 1;58(2):146-57. (PMID: <searchLink fieldCode="PM" term="%2210366446%22">10366446)</searchLink><br />Front Cell Dev Biol. 2020 Nov 24;8:603508. (PMID: <searchLink fieldCode="PM" term="%2233330501%22">33330501)</searchLink><br />Proc Natl Acad Sci U S A. 2003 Jul 8;100(14):8478-83. (PMID: <searchLink fieldCode="PM" term="%2212815105%22">12815105)</searchLink><br />Infect Immun. 2015 Dec;83(12):4710-8. (PMID: <searchLink fieldCode="PM" term="%2226416906%22">26416906)</searchLink><br />PLoS One. 2013;8(2):e57090. (PMID: <searchLink fieldCode="PM" term="%2223441233%22">23441233)</searchLink><br />Nat Methods. 2022 Jun;19(6):679-682. (PMID: <searchLink fieldCode="PM" term="%2235637307%22">35637307)</searchLink><br />Infect Immun. 2002 Jun;70(6):2741-51. (PMID: <searchLink fieldCode="PM" term="%2212010958%22">12010958)</searchLink><br />Nucleic Acids Res. 2022 Jul 5;50(W1):W276-W279. (PMID: <searchLink fieldCode="PM" term="%2235412617%22">35412617)</searchLink><br />Microbes Infect. 2002 Mar;4(3):333-40. (PMID: <searchLink fieldCode="PM" term="%2211909744%22">11909744)</searchLink><br />mSphere. 2024 Nov 21;9(11):e0047324. (PMID: <searchLink fieldCode="PM" term="%2239404459%22">39404459)</searchLink><br />J Bacteriol. 2004 Nov;186(21):7344-52. (PMID: <searchLink fieldCode="PM" term="%2215489446%22">15489446)</searchLink><br />Cell Host Microbe. 2017 Jan 11;21(1):113-121. (PMID: <searchLink fieldCode="PM" term="%2228041929%22">28041929)</searchLink><br />Mol Cell. 2018 Aug 16;71(4):637-648.e5. (PMID: <searchLink fieldCode="PM" term="%2230118682%22">30118682)</searchLink><br />Virulence. 2025 Dec;16(1):2503423. (PMID: <searchLink fieldCode="PM" term="%2240353442%22">40353442)</searchLink><br />PLoS Pathog. 2011 Feb;7(2):e1001289. (PMID: <searchLink fieldCode="PM" term="%2221390206%22">21390206)</searchLink><br />PLoS One. 2013 Dec 31;8(12):e83989. (PMID: <searchLink fieldCode="PM" term="%2224391860%22">24391860)</searchLink><br />J Bacteriol. 2014 Apr;196(7):1325-34. (PMID: <searchLink fieldCode="PM" term="%2224443531%22">24443531)</searchLink><br />Mol Cell. 2015 Jan 22;57(2):329-340. (PMID: <searchLink fieldCode="PM" term="%2225616068%22">25616068)</searchLink><br />FEMS Microbiol Rev. 2016 Nov 1;40(6):875-893. (PMID: <searchLink fieldCode="PM" term="%2228201690%22">28201690)</searchLink><br />Nat Methods. 2011 Jun 26;8(8):659-61. (PMID: <searchLink fieldCode="PM" term="%2221706014%22">21706014)</searchLink><br />Infect Immun. 2019 Oct 18;87(11):. (PMID: <searchLink fieldCode="PM" term="%2231405957%22">31405957)</searchLink><br />Microbes Infect. 2018 Aug - Sep;20(7-8):424-431. (PMID: <searchLink fieldCode="PM" term="%2229248634%22">29248634)</searchLink><br />J Struct Biol. 2013 Jan;181(1):82-8. (PMID: <searchLink fieldCode="PM" term="%2223099021%22">23099021)</searchLink><br />Cell Microbiol. 2000 Feb;2(1):35-47. (PMID: <searchLink fieldCode="PM" term="%2211207561%22">11207561)</searchLink><br />PLoS Pathog. 2011 Sep;7(9):e1002258. (PMID: <searchLink fieldCode="PM" term="%2221966270%22">21966270)</searchLink><br />Trends Microbiol. 2016 Jun;24(6):450-462. (PMID: <searchLink fieldCode="PM" term="%2226924068%22">26924068)</searchLink><br />Curr Biol. 2014 Jan 6;24(1):98-103. (PMID: <searchLink fieldCode="PM" term="%2224361066%22">24361066)</searchLink><br />Protein Sci. 2018 Jan;27(1):14-25. (PMID: <searchLink fieldCode="PM" term="%2228710774%22">28710774)</searchLink><br />PLoS Pathog. 2019 Apr 3;15(4):e1007698. (PMID: <searchLink fieldCode="PM" term="%2230943267%22">30943267)</searchLink>
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  Data: R56AI152526 National Institute of Allergy and Infectious Diseases; R01AI122747 National Institute of Allergy and Infectious Diseases
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  Data: <i>Keywords: </i>Chlamydia trachomatis; Flightless; LRRFIP1; LRRFIP2; TMOD; alphafold; host–pathogen interactions; inclusion membrane protein; intracellular bacteria; microbial cell biology; vacuolar bacteria
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        Text: English
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        StartPage: e0195326
    Subjects:
      – SubjectFull: Chlamydia Infections microbiology
        Type: general
      – SubjectFull: Humans
        Type: general
      – SubjectFull: Protein Binding
        Type: general
      – SubjectFull: HeLa Cells
        Type: general
      – SubjectFull: Chlamydia trachomatis genetics
        Type: general
      – SubjectFull: Chlamydia trachomatis metabolism
        Type: general
      – SubjectFull: Chlamydia trachomatis growth & development
        Type: general
      – SubjectFull: Bacterial Proteins metabolism
        Type: general
      – SubjectFull: Bacterial Proteins genetics
        Type: general
      – SubjectFull: Inclusion Bodies microbiology
        Type: general
      – SubjectFull: Inclusion Bodies metabolism
        Type: general
      – SubjectFull: Multiprotein Complexes metabolism
        Type: general
      – SubjectFull: Membrane Proteins metabolism
        Type: general
      – SubjectFull: Membrane Proteins genetics
        Type: general
      – SubjectFull: Host-Pathogen Interactions
        Type: general
    Titles:
      – TitleFull: The Chlamydia trachomatis effector CT226 directly engages LRRFIP1 to recruit a multiprotein complex that limits inclusion size and progeny production.
        Type: main
  BibRelationships:
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      – PersonEntity:
          Name:
            NameFull: Elwell CA
      – PersonEntity:
          Name:
            NameFull: Diallo A
      – PersonEntity:
          Name:
            NameFull: Sixt BS
      – PersonEntity:
          Name:
            NameFull: Sherry J
      – PersonEntity:
          Name:
            NameFull: Pha K
      – PersonEntity:
          Name:
            NameFull: Valdivia RH
      – PersonEntity:
          Name:
            NameFull: Rosenberg O
      – PersonEntity:
          Name:
            NameFull: Verba K
      – PersonEntity:
          Name:
            NameFull: Engel J
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          Dates:
            – D: 14
              M: 10
              Text: 2026 Oct 14
              Type: published
              Y: 2026
          Identifiers:
            – Type: issn-electronic
              Value: 2150-7511
          Numbering:
            – Type: volume
              Value: 17
            – Type: issue
              Value: 10
          Titles:
            – TitleFull: MBio
              Type: main
ResultId 1