Priming mycobacterial ESX-secreted protein B to form a channel-like structure

ESX-1 is a major virulence factor of Mycobacterium tuberculosis, a secretion machinery directly involved in the survival of the microorganism from the immune system defence. It disrupts the phagosome membrane of the host cell through a contact-dependent mechanism. Recently, the structure of the inne...
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Autor*in:	Abril Gijsbers [verfasserIn] Vanesa Vinciauskaite [verfasserIn] Axel Siroy [verfasserIn] Ye Gao [verfasserIn] Giancarlo Tria [verfasserIn] Anjusha Mathew [verfasserIn] Nuria Sánchez-Puig [verfasserIn] Carmen López-Iglesias [verfasserIn] Peter J. Peters [verfasserIn] Raimond B.G. Ravelli [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2021

Schlagwörter:	Cryo-EM EspB ESX-1 Mycobacteria Preferential orientation

Übergeordnetes Werk:	In: Current Research in Structural Biology - Elsevier, 2020, 3(2021), Seite 153-164
Übergeordnetes Werk:	volume:3 ; year:2021 ; pages:153-164

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1016/j.crstbi.2021.06.001

Katalog-ID:	DOAJ086749242

Internformat


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author_variant	a g ag v v vv a s as y g yg g t gt a m am n s p nsp c l i cli p j p pjp r b r rbr
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allfields	10.1016/j.crstbi.2021.06.001 doi (DE-627)DOAJ086749242 (DE-599)DOAJbb17f446d6a54f5087b60bddb7ad8098 DE-627 ger DE-627 rakwb eng QH301-705.5 Abril Gijsbers verfasserin aut Priming mycobacterial ESX-secreted protein B to form a channel-like structure 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ESX-1 is a major virulence factor of Mycobacterium tuberculosis, a secretion machinery directly involved in the survival of the microorganism from the immune system defence. It disrupts the phagosome membrane of the host cell through a contact-dependent mechanism. Recently, the structure of the inner-membrane core complex of the homologous ESX-3 and ESX-5 was resolved; however, the elements involved in the secretion through the outer membrane or those acting on the host cell membrane are unknown. Protein substrates might form this missing element. Here, we describe the oligomerisation process of the ESX-1 substrate EspB, which occurs upon cleavage of its C-terminal region and is favoured by an acidic environment. Cryo-electron microscopy data shows that quaternary structure of EspB is conserved across slow growing species, but not in the fast growing M. smegmatis. EspB assembles into a channel with dimensions and characteristics suitable for the transit of ESX-1 substrates, as shown by the presence of another EspB trapped within. Our results provide insight into the structure and assembly of EspB, and suggests a possible function as a structural element of ESX-1. Cryo-EM EspB ESX-1 Mycobacteria Preferential orientation Biology (General) Vanesa Vinciauskaite verfasserin aut Axel Siroy verfasserin aut Ye Gao verfasserin aut Giancarlo Tria verfasserin aut Anjusha Mathew verfasserin aut Nuria Sánchez-Puig verfasserin aut Carmen López-Iglesias verfasserin aut Peter J. Peters verfasserin aut Raimond B.G. Ravelli verfasserin aut In Current Research in Structural Biology Elsevier, 2020 3(2021), Seite 153-164 (DE-627)1681860821 2665928X nnns volume:3 year:2021 pages:153-164 https://doi.org/10.1016/j.crstbi.2021.06.001 kostenfrei https://doaj.org/article/bb17f446d6a54f5087b60bddb7ad8098 kostenfrei http://www.sciencedirect.com/science/article/pii/S2665928X21000118 kostenfrei https://doaj.org/toc/2665-928X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 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_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 3 2021 153-164
spelling	10.1016/j.crstbi.2021.06.001 doi (DE-627)DOAJ086749242 (DE-599)DOAJbb17f446d6a54f5087b60bddb7ad8098 DE-627 ger DE-627 rakwb eng QH301-705.5 Abril Gijsbers verfasserin aut Priming mycobacterial ESX-secreted protein B to form a channel-like structure 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ESX-1 is a major virulence factor of Mycobacterium tuberculosis, a secretion machinery directly involved in the survival of the microorganism from the immune system defence. It disrupts the phagosome membrane of the host cell through a contact-dependent mechanism. Recently, the structure of the inner-membrane core complex of the homologous ESX-3 and ESX-5 was resolved; however, the elements involved in the secretion through the outer membrane or those acting on the host cell membrane are unknown. Protein substrates might form this missing element. Here, we describe the oligomerisation process of the ESX-1 substrate EspB, which occurs upon cleavage of its C-terminal region and is favoured by an acidic environment. Cryo-electron microscopy data shows that quaternary structure of EspB is conserved across slow growing species, but not in the fast growing M. smegmatis. EspB assembles into a channel with dimensions and characteristics suitable for the transit of ESX-1 substrates, as shown by the presence of another EspB trapped within. Our results provide insight into the structure and assembly of EspB, and suggests a possible function as a structural element of ESX-1. Cryo-EM EspB ESX-1 Mycobacteria Preferential orientation Biology (General) Vanesa Vinciauskaite verfasserin aut Axel Siroy verfasserin aut Ye Gao verfasserin aut Giancarlo Tria verfasserin aut Anjusha Mathew verfasserin aut Nuria Sánchez-Puig verfasserin aut Carmen López-Iglesias verfasserin aut Peter J. Peters verfasserin aut Raimond B.G. Ravelli verfasserin aut In Current Research in Structural Biology Elsevier, 2020 3(2021), Seite 153-164 (DE-627)1681860821 2665928X nnns volume:3 year:2021 pages:153-164 https://doi.org/10.1016/j.crstbi.2021.06.001 kostenfrei https://doaj.org/article/bb17f446d6a54f5087b60bddb7ad8098 kostenfrei http://www.sciencedirect.com/science/article/pii/S2665928X21000118 kostenfrei https://doaj.org/toc/2665-928X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 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_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 3 2021 153-164
allfields_unstemmed	10.1016/j.crstbi.2021.06.001 doi (DE-627)DOAJ086749242 (DE-599)DOAJbb17f446d6a54f5087b60bddb7ad8098 DE-627 ger DE-627 rakwb eng QH301-705.5 Abril Gijsbers verfasserin aut Priming mycobacterial ESX-secreted protein B to form a channel-like structure 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ESX-1 is a major virulence factor of Mycobacterium tuberculosis, a secretion machinery directly involved in the survival of the microorganism from the immune system defence. It disrupts the phagosome membrane of the host cell through a contact-dependent mechanism. Recently, the structure of the inner-membrane core complex of the homologous ESX-3 and ESX-5 was resolved; however, the elements involved in the secretion through the outer membrane or those acting on the host cell membrane are unknown. Protein substrates might form this missing element. Here, we describe the oligomerisation process of the ESX-1 substrate EspB, which occurs upon cleavage of its C-terminal region and is favoured by an acidic environment. Cryo-electron microscopy data shows that quaternary structure of EspB is conserved across slow growing species, but not in the fast growing M. smegmatis. EspB assembles into a channel with dimensions and characteristics suitable for the transit of ESX-1 substrates, as shown by the presence of another EspB trapped within. Our results provide insight into the structure and assembly of EspB, and suggests a possible function as a structural element of ESX-1. Cryo-EM EspB ESX-1 Mycobacteria Preferential orientation Biology (General) Vanesa Vinciauskaite verfasserin aut Axel Siroy verfasserin aut Ye Gao verfasserin aut Giancarlo Tria verfasserin aut Anjusha Mathew verfasserin aut Nuria Sánchez-Puig verfasserin aut Carmen López-Iglesias verfasserin aut Peter J. Peters verfasserin aut Raimond B.G. Ravelli verfasserin aut In Current Research in Structural Biology Elsevier, 2020 3(2021), Seite 153-164 (DE-627)1681860821 2665928X nnns volume:3 year:2021 pages:153-164 https://doi.org/10.1016/j.crstbi.2021.06.001 kostenfrei https://doaj.org/article/bb17f446d6a54f5087b60bddb7ad8098 kostenfrei http://www.sciencedirect.com/science/article/pii/S2665928X21000118 kostenfrei https://doaj.org/toc/2665-928X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 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_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 3 2021 153-164
allfieldsGer	10.1016/j.crstbi.2021.06.001 doi (DE-627)DOAJ086749242 (DE-599)DOAJbb17f446d6a54f5087b60bddb7ad8098 DE-627 ger DE-627 rakwb eng QH301-705.5 Abril Gijsbers verfasserin aut Priming mycobacterial ESX-secreted protein B to form a channel-like structure 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ESX-1 is a major virulence factor of Mycobacterium tuberculosis, a secretion machinery directly involved in the survival of the microorganism from the immune system defence. It disrupts the phagosome membrane of the host cell through a contact-dependent mechanism. Recently, the structure of the inner-membrane core complex of the homologous ESX-3 and ESX-5 was resolved; however, the elements involved in the secretion through the outer membrane or those acting on the host cell membrane are unknown. Protein substrates might form this missing element. Here, we describe the oligomerisation process of the ESX-1 substrate EspB, which occurs upon cleavage of its C-terminal region and is favoured by an acidic environment. Cryo-electron microscopy data shows that quaternary structure of EspB is conserved across slow growing species, but not in the fast growing M. smegmatis. EspB assembles into a channel with dimensions and characteristics suitable for the transit of ESX-1 substrates, as shown by the presence of another EspB trapped within. Our results provide insight into the structure and assembly of EspB, and suggests a possible function as a structural element of ESX-1. Cryo-EM EspB ESX-1 Mycobacteria Preferential orientation Biology (General) Vanesa Vinciauskaite verfasserin aut Axel Siroy verfasserin aut Ye Gao verfasserin aut Giancarlo Tria verfasserin aut Anjusha Mathew verfasserin aut Nuria Sánchez-Puig verfasserin aut Carmen López-Iglesias verfasserin aut Peter J. Peters verfasserin aut Raimond B.G. Ravelli verfasserin aut In Current Research in Structural Biology Elsevier, 2020 3(2021), Seite 153-164 (DE-627)1681860821 2665928X nnns volume:3 year:2021 pages:153-164 https://doi.org/10.1016/j.crstbi.2021.06.001 kostenfrei https://doaj.org/article/bb17f446d6a54f5087b60bddb7ad8098 kostenfrei http://www.sciencedirect.com/science/article/pii/S2665928X21000118 kostenfrei https://doaj.org/toc/2665-928X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 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_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 3 2021 153-164
allfieldsSound	10.1016/j.crstbi.2021.06.001 doi (DE-627)DOAJ086749242 (DE-599)DOAJbb17f446d6a54f5087b60bddb7ad8098 DE-627 ger DE-627 rakwb eng QH301-705.5 Abril Gijsbers verfasserin aut Priming mycobacterial ESX-secreted protein B to form a channel-like structure 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ESX-1 is a major virulence factor of Mycobacterium tuberculosis, a secretion machinery directly involved in the survival of the microorganism from the immune system defence. It disrupts the phagosome membrane of the host cell through a contact-dependent mechanism. Recently, the structure of the inner-membrane core complex of the homologous ESX-3 and ESX-5 was resolved; however, the elements involved in the secretion through the outer membrane or those acting on the host cell membrane are unknown. Protein substrates might form this missing element. Here, we describe the oligomerisation process of the ESX-1 substrate EspB, which occurs upon cleavage of its C-terminal region and is favoured by an acidic environment. Cryo-electron microscopy data shows that quaternary structure of EspB is conserved across slow growing species, but not in the fast growing M. smegmatis. EspB assembles into a channel with dimensions and characteristics suitable for the transit of ESX-1 substrates, as shown by the presence of another EspB trapped within. Our results provide insight into the structure and assembly of EspB, and suggests a possible function as a structural element of ESX-1. Cryo-EM EspB ESX-1 Mycobacteria Preferential orientation Biology (General) Vanesa Vinciauskaite verfasserin aut Axel Siroy verfasserin aut Ye Gao verfasserin aut Giancarlo Tria verfasserin aut Anjusha Mathew verfasserin aut Nuria Sánchez-Puig verfasserin aut Carmen López-Iglesias verfasserin aut Peter J. Peters verfasserin aut Raimond B.G. Ravelli verfasserin aut In Current Research in Structural Biology Elsevier, 2020 3(2021), Seite 153-164 (DE-627)1681860821 2665928X nnns volume:3 year:2021 pages:153-164 https://doi.org/10.1016/j.crstbi.2021.06.001 kostenfrei https://doaj.org/article/bb17f446d6a54f5087b60bddb7ad8098 kostenfrei http://www.sciencedirect.com/science/article/pii/S2665928X21000118 kostenfrei https://doaj.org/toc/2665-928X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 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_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 3 2021 153-164
language	English
source	In Current Research in Structural Biology 3(2021), Seite 153-164 volume:3 year:2021 pages:153-164
sourceStr	In Current Research in Structural Biology 3(2021), Seite 153-164 volume:3 year:2021 pages:153-164
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Cryo-EM EspB ESX-1 Mycobacteria Preferential orientation Biology (General)
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container_title	Current Research in Structural Biology
authorswithroles_txt_mv	Abril Gijsbers @@aut@@ Vanesa Vinciauskaite @@aut@@ Axel Siroy @@aut@@ Ye Gao @@aut@@ Giancarlo Tria @@aut@@ Anjusha Mathew @@aut@@ Nuria Sánchez-Puig @@aut@@ Carmen López-Iglesias @@aut@@ Peter J. Peters @@aut@@ Raimond B.G. Ravelli @@aut@@
publishDateDaySort_date	2021-01-01T00:00:00Z
hierarchy_top_id	1681860821
id	DOAJ086749242
language_de	englisch
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callnumber-first	Q - Science
author	Abril Gijsbers
spellingShingle	Abril Gijsbers misc QH301-705.5 misc Cryo-EM misc EspB misc ESX-1 misc Mycobacteria misc Preferential orientation misc Biology (General) Priming mycobacterial ESX-secreted protein B to form a channel-like structure
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topic_title	QH301-705.5 Priming mycobacterial ESX-secreted protein B to form a channel-like structure Cryo-EM EspB ESX-1 Mycobacteria Preferential orientation
topic	misc QH301-705.5 misc Cryo-EM misc EspB misc ESX-1 misc Mycobacteria misc Preferential orientation misc Biology (General)
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title	Priming mycobacterial ESX-secreted protein B to form a channel-like structure
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title_full	Priming mycobacterial ESX-secreted protein B to form a channel-like structure
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author_browse	Abril Gijsbers Vanesa Vinciauskaite Axel Siroy Ye Gao Giancarlo Tria Anjusha Mathew Nuria Sánchez-Puig Carmen López-Iglesias Peter J. Peters Raimond B.G. Ravelli
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title_sort	priming mycobacterial esx-secreted protein b to form a channel-like structure
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title_auth	Priming mycobacterial ESX-secreted protein B to form a channel-like structure
abstract	ESX-1 is a major virulence factor of Mycobacterium tuberculosis, a secretion machinery directly involved in the survival of the microorganism from the immune system defence. It disrupts the phagosome membrane of the host cell through a contact-dependent mechanism. Recently, the structure of the inner-membrane core complex of the homologous ESX-3 and ESX-5 was resolved; however, the elements involved in the secretion through the outer membrane or those acting on the host cell membrane are unknown. Protein substrates might form this missing element. Here, we describe the oligomerisation process of the ESX-1 substrate EspB, which occurs upon cleavage of its C-terminal region and is favoured by an acidic environment. Cryo-electron microscopy data shows that quaternary structure of EspB is conserved across slow growing species, but not in the fast growing M. smegmatis. EspB assembles into a channel with dimensions and characteristics suitable for the transit of ESX-1 substrates, as shown by the presence of another EspB trapped within. Our results provide insight into the structure and assembly of EspB, and suggests a possible function as a structural element of ESX-1.
abstractGer	ESX-1 is a major virulence factor of Mycobacterium tuberculosis, a secretion machinery directly involved in the survival of the microorganism from the immune system defence. It disrupts the phagosome membrane of the host cell through a contact-dependent mechanism. Recently, the structure of the inner-membrane core complex of the homologous ESX-3 and ESX-5 was resolved; however, the elements involved in the secretion through the outer membrane or those acting on the host cell membrane are unknown. Protein substrates might form this missing element. Here, we describe the oligomerisation process of the ESX-1 substrate EspB, which occurs upon cleavage of its C-terminal region and is favoured by an acidic environment. Cryo-electron microscopy data shows that quaternary structure of EspB is conserved across slow growing species, but not in the fast growing M. smegmatis. EspB assembles into a channel with dimensions and characteristics suitable for the transit of ESX-1 substrates, as shown by the presence of another EspB trapped within. Our results provide insight into the structure and assembly of EspB, and suggests a possible function as a structural element of ESX-1.
abstract_unstemmed	ESX-1 is a major virulence factor of Mycobacterium tuberculosis, a secretion machinery directly involved in the survival of the microorganism from the immune system defence. It disrupts the phagosome membrane of the host cell through a contact-dependent mechanism. Recently, the structure of the inner-membrane core complex of the homologous ESX-3 and ESX-5 was resolved; however, the elements involved in the secretion through the outer membrane or those acting on the host cell membrane are unknown. Protein substrates might form this missing element. Here, we describe the oligomerisation process of the ESX-1 substrate EspB, which occurs upon cleavage of its C-terminal region and is favoured by an acidic environment. Cryo-electron microscopy data shows that quaternary structure of EspB is conserved across slow growing species, but not in the fast growing M. smegmatis. EspB assembles into a channel with dimensions and characteristics suitable for the transit of ESX-1 substrates, as shown by the presence of another EspB trapped within. Our results provide insight into the structure and assembly of EspB, and suggests a possible function as a structural element of ESX-1.
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title_short	Priming mycobacterial ESX-secreted protein B to form a channel-like structure
url	https://doi.org/10.1016/j.crstbi.2021.06.001 https://doaj.org/article/bb17f446d6a54f5087b60bddb7ad8098 http://www.sciencedirect.com/science/article/pii/S2665928X21000118 https://doaj.org/toc/2665-928X
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Priming mycobacterial ESX-secreted protein B to form a channel-like structure

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