Contribution of DEAD-Box RNA Helicase 21 to the Nucleolar Localization of Porcine Circovirus Type 4 Capsid Protein

Porcine circovirus type 4 (PCV4) is a newly emerging pathogen which might be associated with diverse clinical signs, including respiratory and gastrointestinal distress, dermatitis, and various systemic inflammations. The host cellular proteins binding to PCV4 capsid (Cap) protein are still not clea...
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Autor*in:	Jianwei Zhou [verfasserIn] Yuexia Wang [verfasserIn] Yonghui Qiu [verfasserIn] Yongxia Wang [verfasserIn] Xiaoyu Yang [verfasserIn] Changzhe Liu [verfasserIn] Yongyan Shi [verfasserIn] Xufei Feng [verfasserIn] Lei Hou [verfasserIn] Jue Liu [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2022

Schlagwörter:	porcine circovirus type 4 capsid protein nucleolar localization signal DEAD-box RNA helicase 21 nucleolar localization

Übergeordnetes Werk:	In: Frontiers in Microbiology - Frontiers Media S.A., 2011, 13(2022)
Übergeordnetes Werk:	volume:13 ; year:2022

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3389/fmicb.2022.802740

Katalog-ID:	DOAJ047114991

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520			\|a Porcine circovirus type 4 (PCV4) is a newly emerging pathogen which might be associated with diverse clinical signs, including respiratory and gastrointestinal distress, dermatitis, and various systemic inflammations. The host cellular proteins binding to PCV4 capsid (Cap) protein are still not clear. Herein, we found that the PCV4 Cap mediated translocation of DEAD-box RNA helicase 21 (DDX21) to the cytoplasm from the nucleolus and further verified that the nucleolar localization signal (NoLS) of the PCV4 Cap bound directly to the DDX21. The NoLS of PCV4 Cap and 763GSRSNRFQNK772 residues at the C-terminal domain (CTD) of DDX21 were required for this PCV4 Cap/DDX21 interaction. Further studies indicated that the PCV4 Cap NoLS exploited DDX21 to facilitate its nucleolar localization. In summary, our results firstly demonstrated that DDX21 binds directly to the NoLS of the PCV4 Cap thereby contributing to the nucleolar localization of the PCV4 Cap protein.
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allfields	10.3389/fmicb.2022.802740 doi (DE-627)DOAJ047114991 (DE-599)DOAJ9c30afb3f60948f48567bb3c4053f923 DE-627 ger DE-627 rakwb eng QR1-502 Jianwei Zhou verfasserin aut Contribution of DEAD-Box RNA Helicase 21 to the Nucleolar Localization of Porcine Circovirus Type 4 Capsid Protein 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Porcine circovirus type 4 (PCV4) is a newly emerging pathogen which might be associated with diverse clinical signs, including respiratory and gastrointestinal distress, dermatitis, and various systemic inflammations. The host cellular proteins binding to PCV4 capsid (Cap) protein are still not clear. Herein, we found that the PCV4 Cap mediated translocation of DEAD-box RNA helicase 21 (DDX21) to the cytoplasm from the nucleolus and further verified that the nucleolar localization signal (NoLS) of the PCV4 Cap bound directly to the DDX21. The NoLS of PCV4 Cap and 763GSRSNRFQNK772 residues at the C-terminal domain (CTD) of DDX21 were required for this PCV4 Cap/DDX21 interaction. Further studies indicated that the PCV4 Cap NoLS exploited DDX21 to facilitate its nucleolar localization. In summary, our results firstly demonstrated that DDX21 binds directly to the NoLS of the PCV4 Cap thereby contributing to the nucleolar localization of the PCV4 Cap protein. porcine circovirus type 4 capsid protein nucleolar localization signal DEAD-box RNA helicase 21 nucleolar localization Microbiology Jianwei Zhou verfasserin aut Yuexia Wang verfasserin aut Yonghui Qiu verfasserin aut Yongxia Wang verfasserin aut Yongxia Wang verfasserin aut Xiaoyu Yang verfasserin aut Xiaoyu Yang verfasserin aut Changzhe Liu verfasserin aut Changzhe Liu verfasserin aut Yongyan Shi verfasserin aut Yongyan Shi verfasserin aut Xufei Feng verfasserin aut Xufei Feng verfasserin aut Lei Hou verfasserin aut Lei Hou verfasserin aut Jue Liu verfasserin aut Jue Liu verfasserin aut In Frontiers in Microbiology Frontiers Media S.A., 2011 13(2022) (DE-627)642889384 (DE-600)2587354-4 1664302X nnns volume:13 year:2022 https://doi.org/10.3389/fmicb.2022.802740 kostenfrei https://doaj.org/article/9c30afb3f60948f48567bb3c4053f923 kostenfrei https://www.frontiersin.org/articles/10.3389/fmicb.2022.802740/full kostenfrei https://doaj.org/toc/1664-302X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 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_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 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 13 2022
spelling	10.3389/fmicb.2022.802740 doi (DE-627)DOAJ047114991 (DE-599)DOAJ9c30afb3f60948f48567bb3c4053f923 DE-627 ger DE-627 rakwb eng QR1-502 Jianwei Zhou verfasserin aut Contribution of DEAD-Box RNA Helicase 21 to the Nucleolar Localization of Porcine Circovirus Type 4 Capsid Protein 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Porcine circovirus type 4 (PCV4) is a newly emerging pathogen which might be associated with diverse clinical signs, including respiratory and gastrointestinal distress, dermatitis, and various systemic inflammations. The host cellular proteins binding to PCV4 capsid (Cap) protein are still not clear. Herein, we found that the PCV4 Cap mediated translocation of DEAD-box RNA helicase 21 (DDX21) to the cytoplasm from the nucleolus and further verified that the nucleolar localization signal (NoLS) of the PCV4 Cap bound directly to the DDX21. The NoLS of PCV4 Cap and 763GSRSNRFQNK772 residues at the C-terminal domain (CTD) of DDX21 were required for this PCV4 Cap/DDX21 interaction. Further studies indicated that the PCV4 Cap NoLS exploited DDX21 to facilitate its nucleolar localization. In summary, our results firstly demonstrated that DDX21 binds directly to the NoLS of the PCV4 Cap thereby contributing to the nucleolar localization of the PCV4 Cap protein. porcine circovirus type 4 capsid protein nucleolar localization signal DEAD-box RNA helicase 21 nucleolar localization Microbiology Jianwei Zhou verfasserin aut Yuexia Wang verfasserin aut Yonghui Qiu verfasserin aut Yongxia Wang verfasserin aut Yongxia Wang verfasserin aut Xiaoyu Yang verfasserin aut Xiaoyu Yang verfasserin aut Changzhe Liu verfasserin aut Changzhe Liu verfasserin aut Yongyan Shi verfasserin aut Yongyan Shi verfasserin aut Xufei Feng verfasserin aut Xufei Feng verfasserin aut Lei Hou verfasserin aut Lei Hou verfasserin aut Jue Liu verfasserin aut Jue Liu verfasserin aut In Frontiers in Microbiology Frontiers Media S.A., 2011 13(2022) (DE-627)642889384 (DE-600)2587354-4 1664302X nnns volume:13 year:2022 https://doi.org/10.3389/fmicb.2022.802740 kostenfrei https://doaj.org/article/9c30afb3f60948f48567bb3c4053f923 kostenfrei https://www.frontiersin.org/articles/10.3389/fmicb.2022.802740/full kostenfrei https://doaj.org/toc/1664-302X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 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_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 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 13 2022
allfields_unstemmed	10.3389/fmicb.2022.802740 doi (DE-627)DOAJ047114991 (DE-599)DOAJ9c30afb3f60948f48567bb3c4053f923 DE-627 ger DE-627 rakwb eng QR1-502 Jianwei Zhou verfasserin aut Contribution of DEAD-Box RNA Helicase 21 to the Nucleolar Localization of Porcine Circovirus Type 4 Capsid Protein 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Porcine circovirus type 4 (PCV4) is a newly emerging pathogen which might be associated with diverse clinical signs, including respiratory and gastrointestinal distress, dermatitis, and various systemic inflammations. The host cellular proteins binding to PCV4 capsid (Cap) protein are still not clear. Herein, we found that the PCV4 Cap mediated translocation of DEAD-box RNA helicase 21 (DDX21) to the cytoplasm from the nucleolus and further verified that the nucleolar localization signal (NoLS) of the PCV4 Cap bound directly to the DDX21. The NoLS of PCV4 Cap and 763GSRSNRFQNK772 residues at the C-terminal domain (CTD) of DDX21 were required for this PCV4 Cap/DDX21 interaction. Further studies indicated that the PCV4 Cap NoLS exploited DDX21 to facilitate its nucleolar localization. In summary, our results firstly demonstrated that DDX21 binds directly to the NoLS of the PCV4 Cap thereby contributing to the nucleolar localization of the PCV4 Cap protein. porcine circovirus type 4 capsid protein nucleolar localization signal DEAD-box RNA helicase 21 nucleolar localization Microbiology Jianwei Zhou verfasserin aut Yuexia Wang verfasserin aut Yonghui Qiu verfasserin aut Yongxia Wang verfasserin aut Yongxia Wang verfasserin aut Xiaoyu Yang verfasserin aut Xiaoyu Yang verfasserin aut Changzhe Liu verfasserin aut Changzhe Liu verfasserin aut Yongyan Shi verfasserin aut Yongyan Shi verfasserin aut Xufei Feng verfasserin aut Xufei Feng verfasserin aut Lei Hou verfasserin aut Lei Hou verfasserin aut Jue Liu verfasserin aut Jue Liu verfasserin aut In Frontiers in Microbiology Frontiers Media S.A., 2011 13(2022) (DE-627)642889384 (DE-600)2587354-4 1664302X nnns volume:13 year:2022 https://doi.org/10.3389/fmicb.2022.802740 kostenfrei https://doaj.org/article/9c30afb3f60948f48567bb3c4053f923 kostenfrei https://www.frontiersin.org/articles/10.3389/fmicb.2022.802740/full kostenfrei https://doaj.org/toc/1664-302X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 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_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 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 13 2022
allfieldsGer	10.3389/fmicb.2022.802740 doi (DE-627)DOAJ047114991 (DE-599)DOAJ9c30afb3f60948f48567bb3c4053f923 DE-627 ger DE-627 rakwb eng QR1-502 Jianwei Zhou verfasserin aut Contribution of DEAD-Box RNA Helicase 21 to the Nucleolar Localization of Porcine Circovirus Type 4 Capsid Protein 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Porcine circovirus type 4 (PCV4) is a newly emerging pathogen which might be associated with diverse clinical signs, including respiratory and gastrointestinal distress, dermatitis, and various systemic inflammations. The host cellular proteins binding to PCV4 capsid (Cap) protein are still not clear. Herein, we found that the PCV4 Cap mediated translocation of DEAD-box RNA helicase 21 (DDX21) to the cytoplasm from the nucleolus and further verified that the nucleolar localization signal (NoLS) of the PCV4 Cap bound directly to the DDX21. The NoLS of PCV4 Cap and 763GSRSNRFQNK772 residues at the C-terminal domain (CTD) of DDX21 were required for this PCV4 Cap/DDX21 interaction. Further studies indicated that the PCV4 Cap NoLS exploited DDX21 to facilitate its nucleolar localization. In summary, our results firstly demonstrated that DDX21 binds directly to the NoLS of the PCV4 Cap thereby contributing to the nucleolar localization of the PCV4 Cap protein. porcine circovirus type 4 capsid protein nucleolar localization signal DEAD-box RNA helicase 21 nucleolar localization Microbiology Jianwei Zhou verfasserin aut Yuexia Wang verfasserin aut Yonghui Qiu verfasserin aut Yongxia Wang verfasserin aut Yongxia Wang verfasserin aut Xiaoyu Yang verfasserin aut Xiaoyu Yang verfasserin aut Changzhe Liu verfasserin aut Changzhe Liu verfasserin aut Yongyan Shi verfasserin aut Yongyan Shi verfasserin aut Xufei Feng verfasserin aut Xufei Feng verfasserin aut Lei Hou verfasserin aut Lei Hou verfasserin aut Jue Liu verfasserin aut Jue Liu verfasserin aut In Frontiers in Microbiology Frontiers Media S.A., 2011 13(2022) (DE-627)642889384 (DE-600)2587354-4 1664302X nnns volume:13 year:2022 https://doi.org/10.3389/fmicb.2022.802740 kostenfrei https://doaj.org/article/9c30afb3f60948f48567bb3c4053f923 kostenfrei https://www.frontiersin.org/articles/10.3389/fmicb.2022.802740/full kostenfrei https://doaj.org/toc/1664-302X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 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_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 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 13 2022
allfieldsSound	10.3389/fmicb.2022.802740 doi (DE-627)DOAJ047114991 (DE-599)DOAJ9c30afb3f60948f48567bb3c4053f923 DE-627 ger DE-627 rakwb eng QR1-502 Jianwei Zhou verfasserin aut Contribution of DEAD-Box RNA Helicase 21 to the Nucleolar Localization of Porcine Circovirus Type 4 Capsid Protein 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Porcine circovirus type 4 (PCV4) is a newly emerging pathogen which might be associated with diverse clinical signs, including respiratory and gastrointestinal distress, dermatitis, and various systemic inflammations. The host cellular proteins binding to PCV4 capsid (Cap) protein are still not clear. Herein, we found that the PCV4 Cap mediated translocation of DEAD-box RNA helicase 21 (DDX21) to the cytoplasm from the nucleolus and further verified that the nucleolar localization signal (NoLS) of the PCV4 Cap bound directly to the DDX21. The NoLS of PCV4 Cap and 763GSRSNRFQNK772 residues at the C-terminal domain (CTD) of DDX21 were required for this PCV4 Cap/DDX21 interaction. Further studies indicated that the PCV4 Cap NoLS exploited DDX21 to facilitate its nucleolar localization. In summary, our results firstly demonstrated that DDX21 binds directly to the NoLS of the PCV4 Cap thereby contributing to the nucleolar localization of the PCV4 Cap protein. porcine circovirus type 4 capsid protein nucleolar localization signal DEAD-box RNA helicase 21 nucleolar localization Microbiology Jianwei Zhou verfasserin aut Yuexia Wang verfasserin aut Yonghui Qiu verfasserin aut Yongxia Wang verfasserin aut Yongxia Wang verfasserin aut Xiaoyu Yang verfasserin aut Xiaoyu Yang verfasserin aut Changzhe Liu verfasserin aut Changzhe Liu verfasserin aut Yongyan Shi verfasserin aut Yongyan Shi verfasserin aut Xufei Feng verfasserin aut Xufei Feng verfasserin aut Lei Hou verfasserin aut Lei Hou verfasserin aut Jue Liu verfasserin aut Jue Liu verfasserin aut In Frontiers in Microbiology Frontiers Media S.A., 2011 13(2022) (DE-627)642889384 (DE-600)2587354-4 1664302X nnns volume:13 year:2022 https://doi.org/10.3389/fmicb.2022.802740 kostenfrei https://doaj.org/article/9c30afb3f60948f48567bb3c4053f923 kostenfrei https://www.frontiersin.org/articles/10.3389/fmicb.2022.802740/full kostenfrei https://doaj.org/toc/1664-302X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 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_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 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 13 2022
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authorswithroles_txt_mv	Jianwei Zhou @@aut@@ Yuexia Wang @@aut@@ Yonghui Qiu @@aut@@ Yongxia Wang @@aut@@ Xiaoyu Yang @@aut@@ Changzhe Liu @@aut@@ Yongyan Shi @@aut@@ Xufei Feng @@aut@@ Lei Hou @@aut@@ Jue Liu @@aut@@
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callnumber-first	Q - Science
author	Jianwei Zhou
spellingShingle	Jianwei Zhou misc QR1-502 misc porcine circovirus type 4 misc capsid protein misc nucleolar localization signal misc DEAD-box RNA helicase 21 misc nucleolar localization misc Microbiology Contribution of DEAD-Box RNA Helicase 21 to the Nucleolar Localization of Porcine Circovirus Type 4 Capsid Protein
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topic_title	QR1-502 Contribution of DEAD-Box RNA Helicase 21 to the Nucleolar Localization of Porcine Circovirus Type 4 Capsid Protein porcine circovirus type 4 capsid protein nucleolar localization signal DEAD-box RNA helicase 21 nucleolar localization
topic	misc QR1-502 misc porcine circovirus type 4 misc capsid protein misc nucleolar localization signal misc DEAD-box RNA helicase 21 misc nucleolar localization misc Microbiology
topic_unstemmed	misc QR1-502 misc porcine circovirus type 4 misc capsid protein misc nucleolar localization signal misc DEAD-box RNA helicase 21 misc nucleolar localization misc Microbiology
topic_browse	misc QR1-502 misc porcine circovirus type 4 misc capsid protein misc nucleolar localization signal misc DEAD-box RNA helicase 21 misc nucleolar localization misc Microbiology
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title	Contribution of DEAD-Box RNA Helicase 21 to the Nucleolar Localization of Porcine Circovirus Type 4 Capsid Protein
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title_full	Contribution of DEAD-Box RNA Helicase 21 to the Nucleolar Localization of Porcine Circovirus Type 4 Capsid Protein
author_sort	Jianwei Zhou
journal	Frontiers in Microbiology
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author_browse	Jianwei Zhou Yuexia Wang Yonghui Qiu Yongxia Wang Xiaoyu Yang Changzhe Liu Yongyan Shi Xufei Feng Lei Hou Jue Liu
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title_sort	contribution of dead-box rna helicase 21 to the nucleolar localization of porcine circovirus type 4 capsid protein
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title_auth	Contribution of DEAD-Box RNA Helicase 21 to the Nucleolar Localization of Porcine Circovirus Type 4 Capsid Protein
abstract	Porcine circovirus type 4 (PCV4) is a newly emerging pathogen which might be associated with diverse clinical signs, including respiratory and gastrointestinal distress, dermatitis, and various systemic inflammations. The host cellular proteins binding to PCV4 capsid (Cap) protein are still not clear. Herein, we found that the PCV4 Cap mediated translocation of DEAD-box RNA helicase 21 (DDX21) to the cytoplasm from the nucleolus and further verified that the nucleolar localization signal (NoLS) of the PCV4 Cap bound directly to the DDX21. The NoLS of PCV4 Cap and 763GSRSNRFQNK772 residues at the C-terminal domain (CTD) of DDX21 were required for this PCV4 Cap/DDX21 interaction. Further studies indicated that the PCV4 Cap NoLS exploited DDX21 to facilitate its nucleolar localization. In summary, our results firstly demonstrated that DDX21 binds directly to the NoLS of the PCV4 Cap thereby contributing to the nucleolar localization of the PCV4 Cap protein.
abstractGer	Porcine circovirus type 4 (PCV4) is a newly emerging pathogen which might be associated with diverse clinical signs, including respiratory and gastrointestinal distress, dermatitis, and various systemic inflammations. The host cellular proteins binding to PCV4 capsid (Cap) protein are still not clear. Herein, we found that the PCV4 Cap mediated translocation of DEAD-box RNA helicase 21 (DDX21) to the cytoplasm from the nucleolus and further verified that the nucleolar localization signal (NoLS) of the PCV4 Cap bound directly to the DDX21. The NoLS of PCV4 Cap and 763GSRSNRFQNK772 residues at the C-terminal domain (CTD) of DDX21 were required for this PCV4 Cap/DDX21 interaction. Further studies indicated that the PCV4 Cap NoLS exploited DDX21 to facilitate its nucleolar localization. In summary, our results firstly demonstrated that DDX21 binds directly to the NoLS of the PCV4 Cap thereby contributing to the nucleolar localization of the PCV4 Cap protein.
abstract_unstemmed	Porcine circovirus type 4 (PCV4) is a newly emerging pathogen which might be associated with diverse clinical signs, including respiratory and gastrointestinal distress, dermatitis, and various systemic inflammations. The host cellular proteins binding to PCV4 capsid (Cap) protein are still not clear. Herein, we found that the PCV4 Cap mediated translocation of DEAD-box RNA helicase 21 (DDX21) to the cytoplasm from the nucleolus and further verified that the nucleolar localization signal (NoLS) of the PCV4 Cap bound directly to the DDX21. The NoLS of PCV4 Cap and 763GSRSNRFQNK772 residues at the C-terminal domain (CTD) of DDX21 were required for this PCV4 Cap/DDX21 interaction. Further studies indicated that the PCV4 Cap NoLS exploited DDX21 to facilitate its nucleolar localization. In summary, our results firstly demonstrated that DDX21 binds directly to the NoLS of the PCV4 Cap thereby contributing to the nucleolar localization of the PCV4 Cap protein.
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title_short	Contribution of DEAD-Box RNA Helicase 21 to the Nucleolar Localization of Porcine Circovirus Type 4 Capsid Protein
url	https://doi.org/10.3389/fmicb.2022.802740 https://doaj.org/article/9c30afb3f60948f48567bb3c4053f923 https://www.frontiersin.org/articles/10.3389/fmicb.2022.802740/full https://doaj.org/toc/1664-302X
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author2	Jianwei Zhou Yuexia Wang Yonghui Qiu Yongxia Wang Xiaoyu Yang Changzhe Liu Yongyan Shi Xufei Feng Lei Hou Jue Liu
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up_date	2024-07-04T00:05:25.022Z
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The host cellular proteins binding to PCV4 capsid (Cap) protein are still not clear. Herein, we found that the PCV4 Cap mediated translocation of DEAD-box RNA helicase 21 (DDX21) to the cytoplasm from the nucleolus and further verified that the nucleolar localization signal (NoLS) of the PCV4 Cap bound directly to the DDX21. The NoLS of PCV4 Cap and 763GSRSNRFQNK772 residues at the C-terminal domain (CTD) of DDX21 were required for this PCV4 Cap/DDX21 interaction. Further studies indicated that the PCV4 Cap NoLS exploited DDX21 to facilitate its nucleolar localization. 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ind1="0" ind2=" "><subfield code="a">Changzhe Liu</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Changzhe Liu</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Yongyan Shi</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Yongyan Shi</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Xufei Feng</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Xufei Feng</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" 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Contribution of DEAD-Box RNA Helicase 21 to the Nucleolar Localization of Porcine Circovirus Type 4 Capsid Protein

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