<i<Toxoplasma gondii</i< GRA9 Regulates the Activation of NLRP3 Inflammasome to Exert Anti-Septic Effects in Mice

Dense granule proteins (GRAs) are essential components in <i<Toxoplasma gondii</i<, which are suggested to be promising serodiagnostic markers in toxoplasmosis. In this study, we investigated the function of GRA9 in host response and the associated regulatory mechanism, which were unknow...
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Autor*in:	Jae-Sung Kim [verfasserIn] Seok-Jun Mun [verfasserIn] Euni Cho [verfasserIn] Donggyu Kim [verfasserIn] Wooic Son [verfasserIn] Hye-In Jeon [verfasserIn] Hyo Keun Kim [verfasserIn] Kiseok Jang [verfasserIn] Chul-Su Yang [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2020

Schlagwörter:	NLRP3 macrophages polarization sepsis

Übergeordnetes Werk:	In: International Journal of Molecular Sciences - MDPI AG, 2003, 21(2020), 22, p 8437
Übergeordnetes Werk:	volume:21 ; year:2020 ; number:22, p 8437

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc Journal toc

DOI / URN:	10.3390/ijms21228437

Katalog-ID:	DOAJ010414444

Internformat


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520			\|a Dense granule proteins (GRAs) are essential components in <i<Toxoplasma gondii</i<, which are suggested to be promising serodiagnostic markers in toxoplasmosis. In this study, we investigated the function of GRA9 in host response and the associated regulatory mechanism, which were unknown. We found that GRA9 interacts with NLR family pyrin domain containing 3 (NLRP3) involved in inflammation by forming the NLRP3 inflammasome. The C-terminal of GRA9 (GRA9C) is essential for GRA9–NLRP3 interaction by disrupting the NLRP3 inflammasome through blocking the binding of apoptotic speck-containing (ASC)-NLRP3. Notably, Q200 of GRA9C is essential for the interaction of NLRP3 and blocking the conjugation of ASC. Recombinant GRA9C (rGRA9C) showed an anti-inflammatory effect and the elimination of bacteria by converting M1 to M2 macrophages. In vivo, rGRA9C increased the anti-inflammatory and bactericidal effects and subsequent anti-septic activity in CLP- and <i<E. coli-</i< or <i<P. aeruginosa</i<-induced sepsis model mice by increasing M2 polarization. Taken together, our findings defined a role of <i<T. gondii</i< GRA9 associated with NLRP3 in host macrophages, suggesting its potential as a new candidate therapeutic agent for sepsis.
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allfields	10.3390/ijms21228437 doi (DE-627)DOAJ010414444 (DE-599)DOAJ7d3901bf30264f0d8fb68b636c493953 DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Jae-Sung Kim verfasserin aut <i<Toxoplasma gondii</i< GRA9 Regulates the Activation of NLRP3 Inflammasome to Exert Anti-Septic Effects in Mice 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Dense granule proteins (GRAs) are essential components in <i<Toxoplasma gondii</i<, which are suggested to be promising serodiagnostic markers in toxoplasmosis. In this study, we investigated the function of GRA9 in host response and the associated regulatory mechanism, which were unknown. We found that GRA9 interacts with NLR family pyrin domain containing 3 (NLRP3) involved in inflammation by forming the NLRP3 inflammasome. The C-terminal of GRA9 (GRA9C) is essential for GRA9–NLRP3 interaction by disrupting the NLRP3 inflammasome through blocking the binding of apoptotic speck-containing (ASC)-NLRP3. Notably, Q200 of GRA9C is essential for the interaction of NLRP3 and blocking the conjugation of ASC. Recombinant GRA9C (rGRA9C) showed an anti-inflammatory effect and the elimination of bacteria by converting M1 to M2 macrophages. In vivo, rGRA9C increased the anti-inflammatory and bactericidal effects and subsequent anti-septic activity in CLP- and <i<E. coli-</i< or <i<P. aeruginosa</i<-induced sepsis model mice by increasing M2 polarization. Taken together, our findings defined a role of <i<T. gondii</i< GRA9 associated with NLRP3 in host macrophages, suggesting its potential as a new candidate therapeutic agent for sepsis. <i<Toxoplasma gondii</i< GRA9 NLRP3 macrophages polarization sepsis Biology (General) Chemistry Seok-Jun Mun verfasserin aut Euni Cho verfasserin aut Donggyu Kim verfasserin aut Wooic Son verfasserin aut Hye-In Jeon verfasserin aut Hyo Keun Kim verfasserin aut Kiseok Jang verfasserin aut Chul-Su Yang verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 21(2020), 22, p 8437 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:21 year:2020 number:22, p 8437 https://doi.org/10.3390/ijms21228437 kostenfrei https://doaj.org/article/7d3901bf30264f0d8fb68b636c493953 kostenfrei https://www.mdpi.com/1422-0067/21/22/8437 kostenfrei https://doaj.org/toc/1661-6596 Journal toc kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2020 22, p 8437
spelling	10.3390/ijms21228437 doi (DE-627)DOAJ010414444 (DE-599)DOAJ7d3901bf30264f0d8fb68b636c493953 DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Jae-Sung Kim verfasserin aut <i<Toxoplasma gondii</i< GRA9 Regulates the Activation of NLRP3 Inflammasome to Exert Anti-Septic Effects in Mice 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Dense granule proteins (GRAs) are essential components in <i<Toxoplasma gondii</i<, which are suggested to be promising serodiagnostic markers in toxoplasmosis. In this study, we investigated the function of GRA9 in host response and the associated regulatory mechanism, which were unknown. We found that GRA9 interacts with NLR family pyrin domain containing 3 (NLRP3) involved in inflammation by forming the NLRP3 inflammasome. The C-terminal of GRA9 (GRA9C) is essential for GRA9–NLRP3 interaction by disrupting the NLRP3 inflammasome through blocking the binding of apoptotic speck-containing (ASC)-NLRP3. Notably, Q200 of GRA9C is essential for the interaction of NLRP3 and blocking the conjugation of ASC. Recombinant GRA9C (rGRA9C) showed an anti-inflammatory effect and the elimination of bacteria by converting M1 to M2 macrophages. In vivo, rGRA9C increased the anti-inflammatory and bactericidal effects and subsequent anti-septic activity in CLP- and <i<E. coli-</i< or <i<P. aeruginosa</i<-induced sepsis model mice by increasing M2 polarization. Taken together, our findings defined a role of <i<T. gondii</i< GRA9 associated with NLRP3 in host macrophages, suggesting its potential as a new candidate therapeutic agent for sepsis. <i<Toxoplasma gondii</i< GRA9 NLRP3 macrophages polarization sepsis Biology (General) Chemistry Seok-Jun Mun verfasserin aut Euni Cho verfasserin aut Donggyu Kim verfasserin aut Wooic Son verfasserin aut Hye-In Jeon verfasserin aut Hyo Keun Kim verfasserin aut Kiseok Jang verfasserin aut Chul-Su Yang verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 21(2020), 22, p 8437 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:21 year:2020 number:22, p 8437 https://doi.org/10.3390/ijms21228437 kostenfrei https://doaj.org/article/7d3901bf30264f0d8fb68b636c493953 kostenfrei https://www.mdpi.com/1422-0067/21/22/8437 kostenfrei https://doaj.org/toc/1661-6596 Journal toc kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2020 22, p 8437
allfields_unstemmed	10.3390/ijms21228437 doi (DE-627)DOAJ010414444 (DE-599)DOAJ7d3901bf30264f0d8fb68b636c493953 DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Jae-Sung Kim verfasserin aut <i<Toxoplasma gondii</i< GRA9 Regulates the Activation of NLRP3 Inflammasome to Exert Anti-Septic Effects in Mice 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Dense granule proteins (GRAs) are essential components in <i<Toxoplasma gondii</i<, which are suggested to be promising serodiagnostic markers in toxoplasmosis. In this study, we investigated the function of GRA9 in host response and the associated regulatory mechanism, which were unknown. We found that GRA9 interacts with NLR family pyrin domain containing 3 (NLRP3) involved in inflammation by forming the NLRP3 inflammasome. The C-terminal of GRA9 (GRA9C) is essential for GRA9–NLRP3 interaction by disrupting the NLRP3 inflammasome through blocking the binding of apoptotic speck-containing (ASC)-NLRP3. Notably, Q200 of GRA9C is essential for the interaction of NLRP3 and blocking the conjugation of ASC. Recombinant GRA9C (rGRA9C) showed an anti-inflammatory effect and the elimination of bacteria by converting M1 to M2 macrophages. In vivo, rGRA9C increased the anti-inflammatory and bactericidal effects and subsequent anti-septic activity in CLP- and <i<E. coli-</i< or <i<P. aeruginosa</i<-induced sepsis model mice by increasing M2 polarization. Taken together, our findings defined a role of <i<T. gondii</i< GRA9 associated with NLRP3 in host macrophages, suggesting its potential as a new candidate therapeutic agent for sepsis. <i<Toxoplasma gondii</i< GRA9 NLRP3 macrophages polarization sepsis Biology (General) Chemistry Seok-Jun Mun verfasserin aut Euni Cho verfasserin aut Donggyu Kim verfasserin aut Wooic Son verfasserin aut Hye-In Jeon verfasserin aut Hyo Keun Kim verfasserin aut Kiseok Jang verfasserin aut Chul-Su Yang verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 21(2020), 22, p 8437 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:21 year:2020 number:22, p 8437 https://doi.org/10.3390/ijms21228437 kostenfrei https://doaj.org/article/7d3901bf30264f0d8fb68b636c493953 kostenfrei https://www.mdpi.com/1422-0067/21/22/8437 kostenfrei https://doaj.org/toc/1661-6596 Journal toc kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2020 22, p 8437
allfieldsGer	10.3390/ijms21228437 doi (DE-627)DOAJ010414444 (DE-599)DOAJ7d3901bf30264f0d8fb68b636c493953 DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Jae-Sung Kim verfasserin aut <i<Toxoplasma gondii</i< GRA9 Regulates the Activation of NLRP3 Inflammasome to Exert Anti-Septic Effects in Mice 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Dense granule proteins (GRAs) are essential components in <i<Toxoplasma gondii</i<, which are suggested to be promising serodiagnostic markers in toxoplasmosis. In this study, we investigated the function of GRA9 in host response and the associated regulatory mechanism, which were unknown. We found that GRA9 interacts with NLR family pyrin domain containing 3 (NLRP3) involved in inflammation by forming the NLRP3 inflammasome. The C-terminal of GRA9 (GRA9C) is essential for GRA9–NLRP3 interaction by disrupting the NLRP3 inflammasome through blocking the binding of apoptotic speck-containing (ASC)-NLRP3. Notably, Q200 of GRA9C is essential for the interaction of NLRP3 and blocking the conjugation of ASC. Recombinant GRA9C (rGRA9C) showed an anti-inflammatory effect and the elimination of bacteria by converting M1 to M2 macrophages. In vivo, rGRA9C increased the anti-inflammatory and bactericidal effects and subsequent anti-septic activity in CLP- and <i<E. coli-</i< or <i<P. aeruginosa</i<-induced sepsis model mice by increasing M2 polarization. Taken together, our findings defined a role of <i<T. gondii</i< GRA9 associated with NLRP3 in host macrophages, suggesting its potential as a new candidate therapeutic agent for sepsis. <i<Toxoplasma gondii</i< GRA9 NLRP3 macrophages polarization sepsis Biology (General) Chemistry Seok-Jun Mun verfasserin aut Euni Cho verfasserin aut Donggyu Kim verfasserin aut Wooic Son verfasserin aut Hye-In Jeon verfasserin aut Hyo Keun Kim verfasserin aut Kiseok Jang verfasserin aut Chul-Su Yang verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 21(2020), 22, p 8437 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:21 year:2020 number:22, p 8437 https://doi.org/10.3390/ijms21228437 kostenfrei https://doaj.org/article/7d3901bf30264f0d8fb68b636c493953 kostenfrei https://www.mdpi.com/1422-0067/21/22/8437 kostenfrei https://doaj.org/toc/1661-6596 Journal toc kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2020 22, p 8437
allfieldsSound	10.3390/ijms21228437 doi (DE-627)DOAJ010414444 (DE-599)DOAJ7d3901bf30264f0d8fb68b636c493953 DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Jae-Sung Kim verfasserin aut <i<Toxoplasma gondii</i< GRA9 Regulates the Activation of NLRP3 Inflammasome to Exert Anti-Septic Effects in Mice 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Dense granule proteins (GRAs) are essential components in <i<Toxoplasma gondii</i<, which are suggested to be promising serodiagnostic markers in toxoplasmosis. In this study, we investigated the function of GRA9 in host response and the associated regulatory mechanism, which were unknown. We found that GRA9 interacts with NLR family pyrin domain containing 3 (NLRP3) involved in inflammation by forming the NLRP3 inflammasome. The C-terminal of GRA9 (GRA9C) is essential for GRA9–NLRP3 interaction by disrupting the NLRP3 inflammasome through blocking the binding of apoptotic speck-containing (ASC)-NLRP3. Notably, Q200 of GRA9C is essential for the interaction of NLRP3 and blocking the conjugation of ASC. Recombinant GRA9C (rGRA9C) showed an anti-inflammatory effect and the elimination of bacteria by converting M1 to M2 macrophages. In vivo, rGRA9C increased the anti-inflammatory and bactericidal effects and subsequent anti-septic activity in CLP- and <i<E. coli-</i< or <i<P. aeruginosa</i<-induced sepsis model mice by increasing M2 polarization. Taken together, our findings defined a role of <i<T. gondii</i< GRA9 associated with NLRP3 in host macrophages, suggesting its potential as a new candidate therapeutic agent for sepsis. <i<Toxoplasma gondii</i< GRA9 NLRP3 macrophages polarization sepsis Biology (General) Chemistry Seok-Jun Mun verfasserin aut Euni Cho verfasserin aut Donggyu Kim verfasserin aut Wooic Son verfasserin aut Hye-In Jeon verfasserin aut Hyo Keun Kim verfasserin aut Kiseok Jang verfasserin aut Chul-Su Yang verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 21(2020), 22, p 8437 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:21 year:2020 number:22, p 8437 https://doi.org/10.3390/ijms21228437 kostenfrei https://doaj.org/article/7d3901bf30264f0d8fb68b636c493953 kostenfrei https://www.mdpi.com/1422-0067/21/22/8437 kostenfrei https://doaj.org/toc/1661-6596 Journal toc kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2020 22, p 8437
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source	In International Journal of Molecular Sciences 21(2020), 22, p 8437 volume:21 year:2020 number:22, p 8437
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topic_title	QH301-705.5 QD1-999 <i<Toxoplasma gondii</i< GRA9 Regulates the Activation of NLRP3 Inflammasome to Exert Anti-Septic Effects in Mice <i<Toxoplasma gondii</i< GRA9 NLRP3 macrophages polarization sepsis
topic	misc QH301-705.5 misc QD1-999 misc <i<Toxoplasma gondii</i< GRA9 misc NLRP3 misc macrophages polarization misc sepsis misc Biology (General) misc Chemistry
topic_unstemmed	misc QH301-705.5 misc QD1-999 misc <i<Toxoplasma gondii</i< GRA9 misc NLRP3 misc macrophages polarization misc sepsis misc Biology (General) misc Chemistry
topic_browse	misc QH301-705.5 misc QD1-999 misc <i<Toxoplasma gondii</i< GRA9 misc NLRP3 misc macrophages polarization misc sepsis misc Biology (General) misc Chemistry
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title	<i<Toxoplasma gondii</i< GRA9 Regulates the Activation of NLRP3 Inflammasome to Exert Anti-Septic Effects in Mice
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title_full	<i<Toxoplasma gondii</i< GRA9 Regulates the Activation of NLRP3 Inflammasome to Exert Anti-Septic Effects in Mice
author_sort	Jae-Sung Kim
journal	International Journal of Molecular Sciences
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author_browse	Jae-Sung Kim Seok-Jun Mun Euni Cho Donggyu Kim Wooic Son Hye-In Jeon Hyo Keun Kim Kiseok Jang Chul-Su Yang
container_volume	21
class	QH301-705.5 QD1-999
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author-letter	Jae-Sung Kim
doi_str_mv	10.3390/ijms21228437
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title_sort	<i<toxoplasma gondii</i< gra9 regulates the activation of nlrp3 inflammasome to exert anti-septic effects in mice
callnumber	QH301-705.5
title_auth	<i<Toxoplasma gondii</i< GRA9 Regulates the Activation of NLRP3 Inflammasome to Exert Anti-Septic Effects in Mice
abstract	Dense granule proteins (GRAs) are essential components in <i<Toxoplasma gondii</i<, which are suggested to be promising serodiagnostic markers in toxoplasmosis. In this study, we investigated the function of GRA9 in host response and the associated regulatory mechanism, which were unknown. We found that GRA9 interacts with NLR family pyrin domain containing 3 (NLRP3) involved in inflammation by forming the NLRP3 inflammasome. The C-terminal of GRA9 (GRA9C) is essential for GRA9–NLRP3 interaction by disrupting the NLRP3 inflammasome through blocking the binding of apoptotic speck-containing (ASC)-NLRP3. Notably, Q200 of GRA9C is essential for the interaction of NLRP3 and blocking the conjugation of ASC. Recombinant GRA9C (rGRA9C) showed an anti-inflammatory effect and the elimination of bacteria by converting M1 to M2 macrophages. In vivo, rGRA9C increased the anti-inflammatory and bactericidal effects and subsequent anti-septic activity in CLP- and <i<E. coli-</i< or <i<P. aeruginosa</i<-induced sepsis model mice by increasing M2 polarization. Taken together, our findings defined a role of <i<T. gondii</i< GRA9 associated with NLRP3 in host macrophages, suggesting its potential as a new candidate therapeutic agent for sepsis.
abstractGer	Dense granule proteins (GRAs) are essential components in <i<Toxoplasma gondii</i<, which are suggested to be promising serodiagnostic markers in toxoplasmosis. In this study, we investigated the function of GRA9 in host response and the associated regulatory mechanism, which were unknown. We found that GRA9 interacts with NLR family pyrin domain containing 3 (NLRP3) involved in inflammation by forming the NLRP3 inflammasome. The C-terminal of GRA9 (GRA9C) is essential for GRA9–NLRP3 interaction by disrupting the NLRP3 inflammasome through blocking the binding of apoptotic speck-containing (ASC)-NLRP3. Notably, Q200 of GRA9C is essential for the interaction of NLRP3 and blocking the conjugation of ASC. Recombinant GRA9C (rGRA9C) showed an anti-inflammatory effect and the elimination of bacteria by converting M1 to M2 macrophages. In vivo, rGRA9C increased the anti-inflammatory and bactericidal effects and subsequent anti-septic activity in CLP- and <i<E. coli-</i< or <i<P. aeruginosa</i<-induced sepsis model mice by increasing M2 polarization. Taken together, our findings defined a role of <i<T. gondii</i< GRA9 associated with NLRP3 in host macrophages, suggesting its potential as a new candidate therapeutic agent for sepsis.
abstract_unstemmed	Dense granule proteins (GRAs) are essential components in <i<Toxoplasma gondii</i<, which are suggested to be promising serodiagnostic markers in toxoplasmosis. In this study, we investigated the function of GRA9 in host response and the associated regulatory mechanism, which were unknown. We found that GRA9 interacts with NLR family pyrin domain containing 3 (NLRP3) involved in inflammation by forming the NLRP3 inflammasome. The C-terminal of GRA9 (GRA9C) is essential for GRA9–NLRP3 interaction by disrupting the NLRP3 inflammasome through blocking the binding of apoptotic speck-containing (ASC)-NLRP3. Notably, Q200 of GRA9C is essential for the interaction of NLRP3 and blocking the conjugation of ASC. Recombinant GRA9C (rGRA9C) showed an anti-inflammatory effect and the elimination of bacteria by converting M1 to M2 macrophages. In vivo, rGRA9C increased the anti-inflammatory and bactericidal effects and subsequent anti-septic activity in CLP- and <i<E. coli-</i< or <i<P. aeruginosa</i<-induced sepsis model mice by increasing M2 polarization. Taken together, our findings defined a role of <i<T. gondii</i< GRA9 associated with NLRP3 in host macrophages, suggesting its potential as a new candidate therapeutic agent for sepsis.
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container_issue	22, p 8437
title_short	<i<Toxoplasma gondii</i< GRA9 Regulates the Activation of NLRP3 Inflammasome to Exert Anti-Septic Effects in Mice
url	https://doi.org/10.3390/ijms21228437 https://doaj.org/article/7d3901bf30264f0d8fb68b636c493953 https://www.mdpi.com/1422-0067/21/22/8437 https://doaj.org/toc/1661-6596 https://doaj.org/toc/1422-0067
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