AtaT Improves the Stability of Pore-Forming Protein EspB by Acetylating Lysine 206 to Enhance Strain Virulence

A novel type II toxin of toxin–antitoxin systems (TAs), Gcn5-related N-acetyltransferase (GNAT) family, was reported recently. GNAT toxins are mainly present in pathogenic species, but studies of their involvement in pathogenicity are rare. This study discovered that the GANT toxin AtaT in enterohem...
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Autor*in:	Zhili He [verfasserIn] Tao Li [verfasserIn] Jianxin Wang [verfasserIn] Deyan Luo [verfasserIn] Nianzhi Ning [verfasserIn] Zhan Li [verfasserIn] Fanghong Chen [verfasserIn] Hui Wang [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2021

Schlagwörter:	Gcn5-related N-acetyltransferase AtaT enterohemorrhagic Escherichia coli EspB virulence

Übergeordnetes Werk:	In: Frontiers in Microbiology - Frontiers Media S.A., 2011, 12(2021)
Übergeordnetes Werk:	volume:12 ; year:2021

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3389/fmicb.2021.627141

Katalog-ID:	DOAJ014780240

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allfieldsSound	10.3389/fmicb.2021.627141 doi (DE-627)DOAJ014780240 (DE-599)DOAJ369e5cc33cc04656b514d70794cd1068 DE-627 ger DE-627 rakwb eng QR1-502 Zhili He verfasserin aut AtaT Improves the Stability of Pore-Forming Protein EspB by Acetylating Lysine 206 to Enhance Strain Virulence 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier A novel type II toxin of toxin–antitoxin systems (TAs), Gcn5-related N-acetyltransferase (GNAT) family, was reported recently. GNAT toxins are mainly present in pathogenic species, but studies of their involvement in pathogenicity are rare. This study discovered that the GANT toxin AtaT in enterohemorrhagic Escherichia coli (EHEC) can significantly enhance strain pathogenicity. First, we detected the virulence of ΔataT and ΔataR in cell and animal models. In the absence of ataT, strains showed a lower adhesion number, and host cells presented weaker attaching and effacing lesions, inflammatory response, and pathological injury. Next, we screened the acetylation substrate of AtaT to understand the underlying mechanism. Results showed that E. coli pore-forming protein EspB, which acts as a translocon in type III secretion system (T3SS) in strains, can be acetylated specifically by AtaT. The acetylation of K206 in EspB increases protein stability and maintains the efficiency of effectors translocating into host cells to cause close adhesion and tissue damage. Gcn5-related N-acetyltransferase AtaT enterohemorrhagic Escherichia coli EspB virulence Microbiology Tao Li verfasserin aut Jianxin Wang verfasserin aut Deyan Luo verfasserin aut Nianzhi Ning verfasserin aut Zhan Li verfasserin aut Fanghong Chen verfasserin aut Hui Wang verfasserin aut In Frontiers in Microbiology Frontiers Media S.A., 2011 12(2021) (DE-627)642889384 (DE-600)2587354-4 1664302X nnns volume:12 year:2021 https://doi.org/10.3389/fmicb.2021.627141 kostenfrei https://doaj.org/article/369e5cc33cc04656b514d70794cd1068 kostenfrei https://www.frontiersin.org/articles/10.3389/fmicb.2021.627141/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 12 2021
language	English
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topic_facet	Gcn5-related N-acetyltransferase AtaT enterohemorrhagic Escherichia coli EspB virulence Microbiology
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container_title	Frontiers in Microbiology
authorswithroles_txt_mv	Zhili He @@aut@@ Tao Li @@aut@@ Jianxin Wang @@aut@@ Deyan Luo @@aut@@ Nianzhi Ning @@aut@@ Zhan Li @@aut@@ Fanghong Chen @@aut@@ Hui Wang @@aut@@
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callnumber-first	Q - Science
author	Zhili He
spellingShingle	Zhili He misc QR1-502 misc Gcn5-related N-acetyltransferase misc AtaT misc enterohemorrhagic Escherichia coli misc EspB misc virulence misc Microbiology AtaT Improves the Stability of Pore-Forming Protein EspB by Acetylating Lysine 206 to Enhance Strain Virulence
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topic_title	QR1-502 AtaT Improves the Stability of Pore-Forming Protein EspB by Acetylating Lysine 206 to Enhance Strain Virulence Gcn5-related N-acetyltransferase AtaT enterohemorrhagic Escherichia coli EspB virulence
topic	misc QR1-502 misc Gcn5-related N-acetyltransferase misc AtaT misc enterohemorrhagic Escherichia coli misc EspB misc virulence misc Microbiology
topic_unstemmed	misc QR1-502 misc Gcn5-related N-acetyltransferase misc AtaT misc enterohemorrhagic Escherichia coli misc EspB misc virulence misc Microbiology
topic_browse	misc QR1-502 misc Gcn5-related N-acetyltransferase misc AtaT misc enterohemorrhagic Escherichia coli misc EspB misc virulence misc Microbiology
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title	AtaT Improves the Stability of Pore-Forming Protein EspB by Acetylating Lysine 206 to Enhance Strain Virulence
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title_full	AtaT Improves the Stability of Pore-Forming Protein EspB by Acetylating Lysine 206 to Enhance Strain Virulence
author_sort	Zhili He
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author_browse	Zhili He Tao Li Jianxin Wang Deyan Luo Nianzhi Ning Zhan Li Fanghong Chen Hui Wang
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title_sort	atat improves the stability of pore-forming protein espb by acetylating lysine 206 to enhance strain virulence
callnumber	QR1-502
title_auth	AtaT Improves the Stability of Pore-Forming Protein EspB by Acetylating Lysine 206 to Enhance Strain Virulence
abstract	A novel type II toxin of toxin–antitoxin systems (TAs), Gcn5-related N-acetyltransferase (GNAT) family, was reported recently. GNAT toxins are mainly present in pathogenic species, but studies of their involvement in pathogenicity are rare. This study discovered that the GANT toxin AtaT in enterohemorrhagic Escherichia coli (EHEC) can significantly enhance strain pathogenicity. First, we detected the virulence of ΔataT and ΔataR in cell and animal models. In the absence of ataT, strains showed a lower adhesion number, and host cells presented weaker attaching and effacing lesions, inflammatory response, and pathological injury. Next, we screened the acetylation substrate of AtaT to understand the underlying mechanism. Results showed that E. coli pore-forming protein EspB, which acts as a translocon in type III secretion system (T3SS) in strains, can be acetylated specifically by AtaT. The acetylation of K206 in EspB increases protein stability and maintains the efficiency of effectors translocating into host cells to cause close adhesion and tissue damage.
abstractGer	A novel type II toxin of toxin–antitoxin systems (TAs), Gcn5-related N-acetyltransferase (GNAT) family, was reported recently. GNAT toxins are mainly present in pathogenic species, but studies of their involvement in pathogenicity are rare. This study discovered that the GANT toxin AtaT in enterohemorrhagic Escherichia coli (EHEC) can significantly enhance strain pathogenicity. First, we detected the virulence of ΔataT and ΔataR in cell and animal models. In the absence of ataT, strains showed a lower adhesion number, and host cells presented weaker attaching and effacing lesions, inflammatory response, and pathological injury. Next, we screened the acetylation substrate of AtaT to understand the underlying mechanism. Results showed that E. coli pore-forming protein EspB, which acts as a translocon in type III secretion system (T3SS) in strains, can be acetylated specifically by AtaT. The acetylation of K206 in EspB increases protein stability and maintains the efficiency of effectors translocating into host cells to cause close adhesion and tissue damage.
abstract_unstemmed	A novel type II toxin of toxin–antitoxin systems (TAs), Gcn5-related N-acetyltransferase (GNAT) family, was reported recently. GNAT toxins are mainly present in pathogenic species, but studies of their involvement in pathogenicity are rare. This study discovered that the GANT toxin AtaT in enterohemorrhagic Escherichia coli (EHEC) can significantly enhance strain pathogenicity. First, we detected the virulence of ΔataT and ΔataR in cell and animal models. In the absence of ataT, strains showed a lower adhesion number, and host cells presented weaker attaching and effacing lesions, inflammatory response, and pathological injury. Next, we screened the acetylation substrate of AtaT to understand the underlying mechanism. Results showed that E. coli pore-forming protein EspB, which acts as a translocon in type III secretion system (T3SS) in strains, can be acetylated specifically by AtaT. The acetylation of K206 in EspB increases protein stability and maintains the efficiency of effectors translocating into host cells to cause close adhesion and tissue damage.
collection_details	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
title_short	AtaT Improves the Stability of Pore-Forming Protein EspB by Acetylating Lysine 206 to Enhance Strain Virulence
url	https://doi.org/10.3389/fmicb.2021.627141 https://doaj.org/article/369e5cc33cc04656b514d70794cd1068 https://www.frontiersin.org/articles/10.3389/fmicb.2021.627141/full https://doaj.org/toc/1664-302X
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up_date	2024-07-04T00:27:30.294Z
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