Tick Importin-α Is Implicated in the Interactome and Regulome of the Cofactor Subolesin

Ticks and tick-borne diseases (TBDs) represent a burden for human and animal health worldwide. Currently, vaccines constitute the safest and most effective approach to control ticks and TBDs. Subolesin (SUB) has been identified as a vaccine antigen for the control of tick infestations and pathogen infection and transmission. The characterization of the molecular function of SUB and the identification of tick proteins interacting with SUB may provide the basis for the discovery of novel antigens and for the rational design of novel anti-tick vaccines. In the present study, we used the yeast two-hybrid system (Y2H) as an unbiased approach to identify tick SUB-interacting proteins in an <i<Ixodes ricinus</i< cDNA library, and studied the possible role of SUB as a chromatin remodeler through direct interaction with histones. The Y2H screening identified Importin-α as a potential SUB-interacting protein, which was confirmed in vitro in a protein pull-down assay. The <i<sub</i< gene expression levels in tick midgut and fat body were significantly higher in unfed than fed female ticks, however, the <i<importin-α</i< expression levels did not vary between unfed and fed ticks but tended to be higher in the ovary when compared to those in other organs. The effect of <i<importin-α</i< RNAi was characterized in <i<I. ricinus</i< under artificial feeding conditions. Both <i<sub</i< and <i<importin-α</i< gene knockdown was observed in all tick tissues and, while tick weight was significantly lower in <i<sub</i< RNAi-treated ticks than in controls, <i<importin-α</i< RNAi did not affect tick feeding or oviposition, suggesting that SUB is able to exert its function in the absence of Importin-α. Furthermore, SUB was shown to physically interact with histone 4, which was corroborated by protein pull-down and western blot analysis. These results confirm that by interacting with numerous tick proteins, SUB is a key cofactor of the tick interactome and regulome. Further studies are needed to elucidate the nature of the SUB-Importin-α interaction and the biological processes and functional implications that this interaction may have. Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Sara Artigas-Jerónimo [verfasserIn] Margarita Villar [verfasserIn] Alejandro Cabezas-Cruz [verfasserIn] Grégory Caignard [verfasserIn] Damien Vitour [verfasserIn] Jennifer Richardson [verfasserIn] Sandrine Lacour [verfasserIn] Houssam Attoui [verfasserIn] Lesley Bell-Sakyi [verfasserIn] Eleonore Allain [verfasserIn] Ard M. Nijhof [verfasserIn] Nina Militzer [verfasserIn] Sophia Pinecki Socias [verfasserIn] José de la Fuente [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2021

Schlagwörter:	subolesin interactome regulome importin histone epigenetic

Übergeordnetes Werk:	In: Pathogens - MDPI AG, 2012, 10(2021), 4, p 457
Übergeordnetes Werk:	volume:10 ; year:2021 ; number:4, p 457

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/pathogens10040457

Katalog-ID:	DOAJ085513385

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520			\|a Ticks and tick-borne diseases (TBDs) represent a burden for human and animal health worldwide. Currently, vaccines constitute the safest and most effective approach to control ticks and TBDs. Subolesin (SUB) has been identified as a vaccine antigen for the control of tick infestations and pathogen infection and transmission. The characterization of the molecular function of SUB and the identification of tick proteins interacting with SUB may provide the basis for the discovery of novel antigens and for the rational design of novel anti-tick vaccines. In the present study, we used the yeast two-hybrid system (Y2H) as an unbiased approach to identify tick SUB-interacting proteins in an <i<Ixodes ricinus</i< cDNA library, and studied the possible role of SUB as a chromatin remodeler through direct interaction with histones. The Y2H screening identified Importin-α as a potential SUB-interacting protein, which was confirmed in vitro in a protein pull-down assay. The <i<sub</i< gene expression levels in tick midgut and fat body were significantly higher in unfed than fed female ticks, however, the <i<importin-α</i< expression levels did not vary between unfed and fed ticks but tended to be higher in the ovary when compared to those in other organs. The effect of <i<importin-α</i< RNAi was characterized in <i<I. ricinus</i< under artificial feeding conditions. Both <i<sub</i< and <i<importin-α</i< gene knockdown was observed in all tick tissues and, while tick weight was significantly lower in <i<sub</i< RNAi-treated ticks than in controls, <i<importin-α</i< RNAi did not affect tick feeding or oviposition, suggesting that SUB is able to exert its function in the absence of Importin-α. Furthermore, SUB was shown to physically interact with histone 4, which was corroborated by protein pull-down and western blot analysis. These results confirm that by interacting with numerous tick proteins, SUB is a key cofactor of the tick interactome and regulome. Further studies are needed to elucidate the nature of the SUB-Importin-α interaction and the biological processes and functional implications that this interaction may have.
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allfields	10.3390/pathogens10040457 doi (DE-627)DOAJ085513385 (DE-599)DOAJc3ebbe5d34c54e919613db929f2ea231 DE-627 ger DE-627 rakwb eng Sara Artigas-Jerónimo verfasserin aut Tick Importin-α Is Implicated in the Interactome and Regulome of the Cofactor Subolesin 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ticks and tick-borne diseases (TBDs) represent a burden for human and animal health worldwide. Currently, vaccines constitute the safest and most effective approach to control ticks and TBDs. Subolesin (SUB) has been identified as a vaccine antigen for the control of tick infestations and pathogen infection and transmission. The characterization of the molecular function of SUB and the identification of tick proteins interacting with SUB may provide the basis for the discovery of novel antigens and for the rational design of novel anti-tick vaccines. In the present study, we used the yeast two-hybrid system (Y2H) as an unbiased approach to identify tick SUB-interacting proteins in an <i<Ixodes ricinus</i< cDNA library, and studied the possible role of SUB as a chromatin remodeler through direct interaction with histones. The Y2H screening identified Importin-α as a potential SUB-interacting protein, which was confirmed in vitro in a protein pull-down assay. The <i<sub</i< gene expression levels in tick midgut and fat body were significantly higher in unfed than fed female ticks, however, the <i<importin-α</i< expression levels did not vary between unfed and fed ticks but tended to be higher in the ovary when compared to those in other organs. The effect of <i<importin-α</i< RNAi was characterized in <i<I. ricinus</i< under artificial feeding conditions. Both <i<sub</i< and <i<importin-α</i< gene knockdown was observed in all tick tissues and, while tick weight was significantly lower in <i<sub</i< RNAi-treated ticks than in controls, <i<importin-α</i< RNAi did not affect tick feeding or oviposition, suggesting that SUB is able to exert its function in the absence of Importin-α. Furthermore, SUB was shown to physically interact with histone 4, which was corroborated by protein pull-down and western blot analysis. These results confirm that by interacting with numerous tick proteins, SUB is a key cofactor of the tick interactome and regulome. Further studies are needed to elucidate the nature of the SUB-Importin-α interaction and the biological processes and functional implications that this interaction may have. subolesin interactome regulome importin histone epigenetic Medicine R Margarita Villar verfasserin aut Alejandro Cabezas-Cruz verfasserin aut Grégory Caignard verfasserin aut Damien Vitour verfasserin aut Jennifer Richardson verfasserin aut Sandrine Lacour verfasserin aut Houssam Attoui verfasserin aut Lesley Bell-Sakyi verfasserin aut Eleonore Allain verfasserin aut Ard M. Nijhof verfasserin aut Nina Militzer verfasserin aut Sophia Pinecki Socias verfasserin aut José de la Fuente verfasserin aut In Pathogens MDPI AG, 2012 10(2021), 4, p 457 (DE-627)732627885 (DE-600)2695572-6 20760817 nnns volume:10 year:2021 number:4, p 457 https://doi.org/10.3390/pathogens10040457 kostenfrei https://doaj.org/article/c3ebbe5d34c54e919613db929f2ea231 kostenfrei https://www.mdpi.com/2076-0817/10/4/457 kostenfrei https://doaj.org/toc/2076-0817 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 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_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 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 10 2021 4, p 457
spelling	10.3390/pathogens10040457 doi (DE-627)DOAJ085513385 (DE-599)DOAJc3ebbe5d34c54e919613db929f2ea231 DE-627 ger DE-627 rakwb eng Sara Artigas-Jerónimo verfasserin aut Tick Importin-α Is Implicated in the Interactome and Regulome of the Cofactor Subolesin 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ticks and tick-borne diseases (TBDs) represent a burden for human and animal health worldwide. Currently, vaccines constitute the safest and most effective approach to control ticks and TBDs. Subolesin (SUB) has been identified as a vaccine antigen for the control of tick infestations and pathogen infection and transmission. The characterization of the molecular function of SUB and the identification of tick proteins interacting with SUB may provide the basis for the discovery of novel antigens and for the rational design of novel anti-tick vaccines. In the present study, we used the yeast two-hybrid system (Y2H) as an unbiased approach to identify tick SUB-interacting proteins in an <i<Ixodes ricinus</i< cDNA library, and studied the possible role of SUB as a chromatin remodeler through direct interaction with histones. The Y2H screening identified Importin-α as a potential SUB-interacting protein, which was confirmed in vitro in a protein pull-down assay. The <i<sub</i< gene expression levels in tick midgut and fat body were significantly higher in unfed than fed female ticks, however, the <i<importin-α</i< expression levels did not vary between unfed and fed ticks but tended to be higher in the ovary when compared to those in other organs. The effect of <i<importin-α</i< RNAi was characterized in <i<I. ricinus</i< under artificial feeding conditions. Both <i<sub</i< and <i<importin-α</i< gene knockdown was observed in all tick tissues and, while tick weight was significantly lower in <i<sub</i< RNAi-treated ticks than in controls, <i<importin-α</i< RNAi did not affect tick feeding or oviposition, suggesting that SUB is able to exert its function in the absence of Importin-α. Furthermore, SUB was shown to physically interact with histone 4, which was corroborated by protein pull-down and western blot analysis. These results confirm that by interacting with numerous tick proteins, SUB is a key cofactor of the tick interactome and regulome. Further studies are needed to elucidate the nature of the SUB-Importin-α interaction and the biological processes and functional implications that this interaction may have. subolesin interactome regulome importin histone epigenetic Medicine R Margarita Villar verfasserin aut Alejandro Cabezas-Cruz verfasserin aut Grégory Caignard verfasserin aut Damien Vitour verfasserin aut Jennifer Richardson verfasserin aut Sandrine Lacour verfasserin aut Houssam Attoui verfasserin aut Lesley Bell-Sakyi verfasserin aut Eleonore Allain verfasserin aut Ard M. Nijhof verfasserin aut Nina Militzer verfasserin aut Sophia Pinecki Socias verfasserin aut José de la Fuente verfasserin aut In Pathogens MDPI AG, 2012 10(2021), 4, p 457 (DE-627)732627885 (DE-600)2695572-6 20760817 nnns volume:10 year:2021 number:4, p 457 https://doi.org/10.3390/pathogens10040457 kostenfrei https://doaj.org/article/c3ebbe5d34c54e919613db929f2ea231 kostenfrei https://www.mdpi.com/2076-0817/10/4/457 kostenfrei https://doaj.org/toc/2076-0817 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 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_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 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 10 2021 4, p 457
allfields_unstemmed	10.3390/pathogens10040457 doi (DE-627)DOAJ085513385 (DE-599)DOAJc3ebbe5d34c54e919613db929f2ea231 DE-627 ger DE-627 rakwb eng Sara Artigas-Jerónimo verfasserin aut Tick Importin-α Is Implicated in the Interactome and Regulome of the Cofactor Subolesin 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ticks and tick-borne diseases (TBDs) represent a burden for human and animal health worldwide. Currently, vaccines constitute the safest and most effective approach to control ticks and TBDs. Subolesin (SUB) has been identified as a vaccine antigen for the control of tick infestations and pathogen infection and transmission. The characterization of the molecular function of SUB and the identification of tick proteins interacting with SUB may provide the basis for the discovery of novel antigens and for the rational design of novel anti-tick vaccines. In the present study, we used the yeast two-hybrid system (Y2H) as an unbiased approach to identify tick SUB-interacting proteins in an <i<Ixodes ricinus</i< cDNA library, and studied the possible role of SUB as a chromatin remodeler through direct interaction with histones. The Y2H screening identified Importin-α as a potential SUB-interacting protein, which was confirmed in vitro in a protein pull-down assay. The <i<sub</i< gene expression levels in tick midgut and fat body were significantly higher in unfed than fed female ticks, however, the <i<importin-α</i< expression levels did not vary between unfed and fed ticks but tended to be higher in the ovary when compared to those in other organs. The effect of <i<importin-α</i< RNAi was characterized in <i<I. ricinus</i< under artificial feeding conditions. Both <i<sub</i< and <i<importin-α</i< gene knockdown was observed in all tick tissues and, while tick weight was significantly lower in <i<sub</i< RNAi-treated ticks than in controls, <i<importin-α</i< RNAi did not affect tick feeding or oviposition, suggesting that SUB is able to exert its function in the absence of Importin-α. Furthermore, SUB was shown to physically interact with histone 4, which was corroborated by protein pull-down and western blot analysis. These results confirm that by interacting with numerous tick proteins, SUB is a key cofactor of the tick interactome and regulome. Further studies are needed to elucidate the nature of the SUB-Importin-α interaction and the biological processes and functional implications that this interaction may have. subolesin interactome regulome importin histone epigenetic Medicine R Margarita Villar verfasserin aut Alejandro Cabezas-Cruz verfasserin aut Grégory Caignard verfasserin aut Damien Vitour verfasserin aut Jennifer Richardson verfasserin aut Sandrine Lacour verfasserin aut Houssam Attoui verfasserin aut Lesley Bell-Sakyi verfasserin aut Eleonore Allain verfasserin aut Ard M. Nijhof verfasserin aut Nina Militzer verfasserin aut Sophia Pinecki Socias verfasserin aut José de la Fuente verfasserin aut In Pathogens MDPI AG, 2012 10(2021), 4, p 457 (DE-627)732627885 (DE-600)2695572-6 20760817 nnns volume:10 year:2021 number:4, p 457 https://doi.org/10.3390/pathogens10040457 kostenfrei https://doaj.org/article/c3ebbe5d34c54e919613db929f2ea231 kostenfrei https://www.mdpi.com/2076-0817/10/4/457 kostenfrei https://doaj.org/toc/2076-0817 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 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_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 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 10 2021 4, p 457
allfieldsGer	10.3390/pathogens10040457 doi (DE-627)DOAJ085513385 (DE-599)DOAJc3ebbe5d34c54e919613db929f2ea231 DE-627 ger DE-627 rakwb eng Sara Artigas-Jerónimo verfasserin aut Tick Importin-α Is Implicated in the Interactome and Regulome of the Cofactor Subolesin 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ticks and tick-borne diseases (TBDs) represent a burden for human and animal health worldwide. Currently, vaccines constitute the safest and most effective approach to control ticks and TBDs. Subolesin (SUB) has been identified as a vaccine antigen for the control of tick infestations and pathogen infection and transmission. The characterization of the molecular function of SUB and the identification of tick proteins interacting with SUB may provide the basis for the discovery of novel antigens and for the rational design of novel anti-tick vaccines. In the present study, we used the yeast two-hybrid system (Y2H) as an unbiased approach to identify tick SUB-interacting proteins in an <i<Ixodes ricinus</i< cDNA library, and studied the possible role of SUB as a chromatin remodeler through direct interaction with histones. The Y2H screening identified Importin-α as a potential SUB-interacting protein, which was confirmed in vitro in a protein pull-down assay. The <i<sub</i< gene expression levels in tick midgut and fat body were significantly higher in unfed than fed female ticks, however, the <i<importin-α</i< expression levels did not vary between unfed and fed ticks but tended to be higher in the ovary when compared to those in other organs. The effect of <i<importin-α</i< RNAi was characterized in <i<I. ricinus</i< under artificial feeding conditions. Both <i<sub</i< and <i<importin-α</i< gene knockdown was observed in all tick tissues and, while tick weight was significantly lower in <i<sub</i< RNAi-treated ticks than in controls, <i<importin-α</i< RNAi did not affect tick feeding or oviposition, suggesting that SUB is able to exert its function in the absence of Importin-α. Furthermore, SUB was shown to physically interact with histone 4, which was corroborated by protein pull-down and western blot analysis. These results confirm that by interacting with numerous tick proteins, SUB is a key cofactor of the tick interactome and regulome. Further studies are needed to elucidate the nature of the SUB-Importin-α interaction and the biological processes and functional implications that this interaction may have. subolesin interactome regulome importin histone epigenetic Medicine R Margarita Villar verfasserin aut Alejandro Cabezas-Cruz verfasserin aut Grégory Caignard verfasserin aut Damien Vitour verfasserin aut Jennifer Richardson verfasserin aut Sandrine Lacour verfasserin aut Houssam Attoui verfasserin aut Lesley Bell-Sakyi verfasserin aut Eleonore Allain verfasserin aut Ard M. Nijhof verfasserin aut Nina Militzer verfasserin aut Sophia Pinecki Socias verfasserin aut José de la Fuente verfasserin aut In Pathogens MDPI AG, 2012 10(2021), 4, p 457 (DE-627)732627885 (DE-600)2695572-6 20760817 nnns volume:10 year:2021 number:4, p 457 https://doi.org/10.3390/pathogens10040457 kostenfrei https://doaj.org/article/c3ebbe5d34c54e919613db929f2ea231 kostenfrei https://www.mdpi.com/2076-0817/10/4/457 kostenfrei https://doaj.org/toc/2076-0817 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 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_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 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 10 2021 4, p 457
allfieldsSound	10.3390/pathogens10040457 doi (DE-627)DOAJ085513385 (DE-599)DOAJc3ebbe5d34c54e919613db929f2ea231 DE-627 ger DE-627 rakwb eng Sara Artigas-Jerónimo verfasserin aut Tick Importin-α Is Implicated in the Interactome and Regulome of the Cofactor Subolesin 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ticks and tick-borne diseases (TBDs) represent a burden for human and animal health worldwide. Currently, vaccines constitute the safest and most effective approach to control ticks and TBDs. Subolesin (SUB) has been identified as a vaccine antigen for the control of tick infestations and pathogen infection and transmission. The characterization of the molecular function of SUB and the identification of tick proteins interacting with SUB may provide the basis for the discovery of novel antigens and for the rational design of novel anti-tick vaccines. In the present study, we used the yeast two-hybrid system (Y2H) as an unbiased approach to identify tick SUB-interacting proteins in an <i<Ixodes ricinus</i< cDNA library, and studied the possible role of SUB as a chromatin remodeler through direct interaction with histones. The Y2H screening identified Importin-α as a potential SUB-interacting protein, which was confirmed in vitro in a protein pull-down assay. The <i<sub</i< gene expression levels in tick midgut and fat body were significantly higher in unfed than fed female ticks, however, the <i<importin-α</i< expression levels did not vary between unfed and fed ticks but tended to be higher in the ovary when compared to those in other organs. The effect of <i<importin-α</i< RNAi was characterized in <i<I. ricinus</i< under artificial feeding conditions. Both <i<sub</i< and <i<importin-α</i< gene knockdown was observed in all tick tissues and, while tick weight was significantly lower in <i<sub</i< RNAi-treated ticks than in controls, <i<importin-α</i< RNAi did not affect tick feeding or oviposition, suggesting that SUB is able to exert its function in the absence of Importin-α. Furthermore, SUB was shown to physically interact with histone 4, which was corroborated by protein pull-down and western blot analysis. These results confirm that by interacting with numerous tick proteins, SUB is a key cofactor of the tick interactome and regulome. Further studies are needed to elucidate the nature of the SUB-Importin-α interaction and the biological processes and functional implications that this interaction may have. subolesin interactome regulome importin histone epigenetic Medicine R Margarita Villar verfasserin aut Alejandro Cabezas-Cruz verfasserin aut Grégory Caignard verfasserin aut Damien Vitour verfasserin aut Jennifer Richardson verfasserin aut Sandrine Lacour verfasserin aut Houssam Attoui verfasserin aut Lesley Bell-Sakyi verfasserin aut Eleonore Allain verfasserin aut Ard M. Nijhof verfasserin aut Nina Militzer verfasserin aut Sophia Pinecki Socias verfasserin aut José de la Fuente verfasserin aut In Pathogens MDPI AG, 2012 10(2021), 4, p 457 (DE-627)732627885 (DE-600)2695572-6 20760817 nnns volume:10 year:2021 number:4, p 457 https://doi.org/10.3390/pathogens10040457 kostenfrei https://doaj.org/article/c3ebbe5d34c54e919613db929f2ea231 kostenfrei https://www.mdpi.com/2076-0817/10/4/457 kostenfrei https://doaj.org/toc/2076-0817 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 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_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 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 10 2021 4, p 457
language	English
source	In Pathogens 10(2021), 4, p 457 volume:10 year:2021 number:4, p 457
sourceStr	In Pathogens 10(2021), 4, p 457 volume:10 year:2021 number:4, p 457
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	subolesin interactome regulome importin histone epigenetic Medicine R
isfreeaccess_bool	true
container_title	Pathogens
authorswithroles_txt_mv	Sara Artigas-Jerónimo @@aut@@ Margarita Villar @@aut@@ Alejandro Cabezas-Cruz @@aut@@ Grégory Caignard @@aut@@ Damien Vitour @@aut@@ Jennifer Richardson @@aut@@ Sandrine Lacour @@aut@@ Houssam Attoui @@aut@@ Lesley Bell-Sakyi @@aut@@ Eleonore Allain @@aut@@ Ard M. Nijhof @@aut@@ Nina Militzer @@aut@@ Sophia Pinecki Socias @@aut@@ José de la Fuente @@aut@@
publishDateDaySort_date	2021-01-01T00:00:00Z
hierarchy_top_id	732627885
id	DOAJ085513385
language_de	englisch
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Currently, vaccines constitute the safest and most effective approach to control ticks and TBDs. Subolesin (SUB) has been identified as a vaccine antigen for the control of tick infestations and pathogen infection and transmission. The characterization of the molecular function of SUB and the identification of tick proteins interacting with SUB may provide the basis for the discovery of novel antigens and for the rational design of novel anti-tick vaccines. In the present study, we used the yeast two-hybrid system (Y2H) as an unbiased approach to identify tick SUB-interacting proteins in an <i<Ixodes ricinus</i< cDNA library, and studied the possible role of SUB as a chromatin remodeler through direct interaction with histones. The Y2H screening identified Importin-α as a potential SUB-interacting protein, which was confirmed in vitro in a protein pull-down assay. The <i<sub</i< gene expression levels in tick midgut and fat body were significantly higher in unfed than fed female ticks, however, the <i<importin-α</i< expression levels did not vary between unfed and fed ticks but tended to be higher in the ovary when compared to those in other organs. The effect of <i<importin-α</i< RNAi was characterized in <i<I. ricinus</i< under artificial feeding conditions. Both <i<sub</i< and <i<importin-α</i< gene knockdown was observed in all tick tissues and, while tick weight was significantly lower in <i<sub</i< RNAi-treated ticks than in controls, <i<importin-α</i< RNAi did not affect tick feeding or oviposition, suggesting that SUB is able to exert its function in the absence of Importin-α. Furthermore, SUB was shown to physically interact with histone 4, which was corroborated by protein pull-down and western blot analysis. 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author	Sara Artigas-Jerónimo
spellingShingle	Sara Artigas-Jerónimo misc subolesin misc interactome misc regulome misc importin misc histone misc epigenetic misc Medicine misc R Tick Importin-α Is Implicated in the Interactome and Regulome of the Cofactor Subolesin
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topic_title	Tick Importin-α Is Implicated in the Interactome and Regulome of the Cofactor Subolesin subolesin interactome regulome importin histone epigenetic
topic	misc subolesin misc interactome misc regulome misc importin misc histone misc epigenetic misc Medicine misc R
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title	Tick Importin-α Is Implicated in the Interactome and Regulome of the Cofactor Subolesin
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title_full	Tick Importin-α Is Implicated in the Interactome and Regulome of the Cofactor Subolesin
author_sort	Sara Artigas-Jerónimo
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author_browse	Sara Artigas-Jerónimo Margarita Villar Alejandro Cabezas-Cruz Grégory Caignard Damien Vitour Jennifer Richardson Sandrine Lacour Houssam Attoui Lesley Bell-Sakyi Eleonore Allain Ard M. Nijhof Nina Militzer Sophia Pinecki Socias José de la Fuente
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format_se	Elektronische Aufsätze
author-letter	Sara Artigas-Jerónimo
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title_sort	tick importin-α is implicated in the interactome and regulome of the cofactor subolesin
title_auth	Tick Importin-α Is Implicated in the Interactome and Regulome of the Cofactor Subolesin
abstract	Ticks and tick-borne diseases (TBDs) represent a burden for human and animal health worldwide. Currently, vaccines constitute the safest and most effective approach to control ticks and TBDs. Subolesin (SUB) has been identified as a vaccine antigen for the control of tick infestations and pathogen infection and transmission. The characterization of the molecular function of SUB and the identification of tick proteins interacting with SUB may provide the basis for the discovery of novel antigens and for the rational design of novel anti-tick vaccines. In the present study, we used the yeast two-hybrid system (Y2H) as an unbiased approach to identify tick SUB-interacting proteins in an <i<Ixodes ricinus</i< cDNA library, and studied the possible role of SUB as a chromatin remodeler through direct interaction with histones. The Y2H screening identified Importin-α as a potential SUB-interacting protein, which was confirmed in vitro in a protein pull-down assay. The <i<sub</i< gene expression levels in tick midgut and fat body were significantly higher in unfed than fed female ticks, however, the <i<importin-α</i< expression levels did not vary between unfed and fed ticks but tended to be higher in the ovary when compared to those in other organs. The effect of <i<importin-α</i< RNAi was characterized in <i<I. ricinus</i< under artificial feeding conditions. Both <i<sub</i< and <i<importin-α</i< gene knockdown was observed in all tick tissues and, while tick weight was significantly lower in <i<sub</i< RNAi-treated ticks than in controls, <i<importin-α</i< RNAi did not affect tick feeding or oviposition, suggesting that SUB is able to exert its function in the absence of Importin-α. Furthermore, SUB was shown to physically interact with histone 4, which was corroborated by protein pull-down and western blot analysis. These results confirm that by interacting with numerous tick proteins, SUB is a key cofactor of the tick interactome and regulome. Further studies are needed to elucidate the nature of the SUB-Importin-α interaction and the biological processes and functional implications that this interaction may have.
abstractGer	Ticks and tick-borne diseases (TBDs) represent a burden for human and animal health worldwide. Currently, vaccines constitute the safest and most effective approach to control ticks and TBDs. Subolesin (SUB) has been identified as a vaccine antigen for the control of tick infestations and pathogen infection and transmission. The characterization of the molecular function of SUB and the identification of tick proteins interacting with SUB may provide the basis for the discovery of novel antigens and for the rational design of novel anti-tick vaccines. In the present study, we used the yeast two-hybrid system (Y2H) as an unbiased approach to identify tick SUB-interacting proteins in an <i<Ixodes ricinus</i< cDNA library, and studied the possible role of SUB as a chromatin remodeler through direct interaction with histones. The Y2H screening identified Importin-α as a potential SUB-interacting protein, which was confirmed in vitro in a protein pull-down assay. The <i<sub</i< gene expression levels in tick midgut and fat body were significantly higher in unfed than fed female ticks, however, the <i<importin-α</i< expression levels did not vary between unfed and fed ticks but tended to be higher in the ovary when compared to those in other organs. The effect of <i<importin-α</i< RNAi was characterized in <i<I. ricinus</i< under artificial feeding conditions. Both <i<sub</i< and <i<importin-α</i< gene knockdown was observed in all tick tissues and, while tick weight was significantly lower in <i<sub</i< RNAi-treated ticks than in controls, <i<importin-α</i< RNAi did not affect tick feeding or oviposition, suggesting that SUB is able to exert its function in the absence of Importin-α. Furthermore, SUB was shown to physically interact with histone 4, which was corroborated by protein pull-down and western blot analysis. These results confirm that by interacting with numerous tick proteins, SUB is a key cofactor of the tick interactome and regulome. Further studies are needed to elucidate the nature of the SUB-Importin-α interaction and the biological processes and functional implications that this interaction may have.
abstract_unstemmed	Ticks and tick-borne diseases (TBDs) represent a burden for human and animal health worldwide. Currently, vaccines constitute the safest and most effective approach to control ticks and TBDs. Subolesin (SUB) has been identified as a vaccine antigen for the control of tick infestations and pathogen infection and transmission. The characterization of the molecular function of SUB and the identification of tick proteins interacting with SUB may provide the basis for the discovery of novel antigens and for the rational design of novel anti-tick vaccines. In the present study, we used the yeast two-hybrid system (Y2H) as an unbiased approach to identify tick SUB-interacting proteins in an <i<Ixodes ricinus</i< cDNA library, and studied the possible role of SUB as a chromatin remodeler through direct interaction with histones. The Y2H screening identified Importin-α as a potential SUB-interacting protein, which was confirmed in vitro in a protein pull-down assay. The <i<sub</i< gene expression levels in tick midgut and fat body were significantly higher in unfed than fed female ticks, however, the <i<importin-α</i< expression levels did not vary between unfed and fed ticks but tended to be higher in the ovary when compared to those in other organs. The effect of <i<importin-α</i< RNAi was characterized in <i<I. ricinus</i< under artificial feeding conditions. Both <i<sub</i< and <i<importin-α</i< gene knockdown was observed in all tick tissues and, while tick weight was significantly lower in <i<sub</i< RNAi-treated ticks than in controls, <i<importin-α</i< RNAi did not affect tick feeding or oviposition, suggesting that SUB is able to exert its function in the absence of Importin-α. Furthermore, SUB was shown to physically interact with histone 4, which was corroborated by protein pull-down and western blot analysis. These results confirm that by interacting with numerous tick proteins, SUB is a key cofactor of the tick interactome and regulome. Further studies are needed to elucidate the nature of the SUB-Importin-α interaction and the biological processes and functional implications that this interaction may have.
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title_short	Tick Importin-α Is Implicated in the Interactome and Regulome of the Cofactor Subolesin
url	https://doi.org/10.3390/pathogens10040457 https://doaj.org/article/c3ebbe5d34c54e919613db929f2ea231 https://www.mdpi.com/2076-0817/10/4/457 https://doaj.org/toc/2076-0817
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author2	Margarita Villar Alejandro Cabezas-Cruz Grégory Caignard Damien Vitour Jennifer Richardson Sandrine Lacour Houssam Attoui Lesley Bell-Sakyi Eleonore Allain Ard M. Nijhof Nina Militzer Sophia Pinecki Socias José de la Fuente
author2Str	Margarita Villar Alejandro Cabezas-Cruz Grégory Caignard Damien Vitour Jennifer Richardson Sandrine Lacour Houssam Attoui Lesley Bell-Sakyi Eleonore Allain Ard M. Nijhof Nina Militzer Sophia Pinecki Socias José de la Fuente
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up_date	2024-07-03T15:11:43.454Z
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score	7.401513

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