BtcA, A class IA type III chaperone, interacts with the BteA N-terminal domain through a globular/non-globular mechanism.

Bordetella pertussis, the etiological agent of "whooping cough" disease, utilizes the type III secretion system (T3SS) to deliver a 69 kDa cytotoxic effector protein, BteA, directly into the host cells. As with other T3SS effectors, prior to its secretion BteA binds BtcA, a 13.9 kDa protei...

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Autores principales:	Chen Guttman, Geula Davidov, Adi Yahalom, Hadassa Shaked, Sofiya Kolusheva, Ronit Bitton, Shiran Barber-Zucker, Jordan H Chill, Raz Zarivach
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/170ed984def44f2d8f50b288c5223983
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spelling	oai:doaj.org-article:170ed984def44f2d8f50b288c52239832021-11-18T08:43:57ZBtcA, A class IA type III chaperone, interacts with the BteA N-terminal domain through a globular/non-globular mechanism.1932-620310.1371/journal.pone.0081557https://doaj.org/article/170ed984def44f2d8f50b288c52239832013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24312558/?tool=EBIhttps://doaj.org/toc/1932-6203Bordetella pertussis, the etiological agent of "whooping cough" disease, utilizes the type III secretion system (T3SS) to deliver a 69 kDa cytotoxic effector protein, BteA, directly into the host cells. As with other T3SS effectors, prior to its secretion BteA binds BtcA, a 13.9 kDa protein predicted to act as a T3SS class IA chaperone. While this interaction had been characterized for such effector-chaperone pairs in other pathogens, it has yet to be fully investigated in Bordetella. Here we provide the first biochemical proof that BtcA is indeed a class IA chaperone, responsible for the binding of BteA's N-terminal domain. We bring forth extensive evidence that BtcA binds its substrate effector through a dual-interface binding mechanism comprising of non-globular and bi-globular interactions at a moderate micromolar level binding affinity. We demonstrate that the non-globular interactions involve the first 31 N-terminal residues of BteA287 and their removal leads to destabilization of the effector-chaperone complex and lower binding affinities to BtcA. These findings represent an important first step towards a molecular understanding of BteA secretion and cell entry.Chen GuttmanGeula DavidovAdi YahalomHadassa ShakedSofiya KolushevaRonit BittonShiran Barber-ZuckerJordan H ChillRaz ZarivachPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 12, p e81557 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Chen Guttman Geula Davidov Adi Yahalom Hadassa Shaked Sofiya Kolusheva Ronit Bitton Shiran Barber-Zucker Jordan H Chill Raz Zarivach BtcA, A class IA type III chaperone, interacts with the BteA N-terminal domain through a globular/non-globular mechanism.
description	Bordetella pertussis, the etiological agent of "whooping cough" disease, utilizes the type III secretion system (T3SS) to deliver a 69 kDa cytotoxic effector protein, BteA, directly into the host cells. As with other T3SS effectors, prior to its secretion BteA binds BtcA, a 13.9 kDa protein predicted to act as a T3SS class IA chaperone. While this interaction had been characterized for such effector-chaperone pairs in other pathogens, it has yet to be fully investigated in Bordetella. Here we provide the first biochemical proof that BtcA is indeed a class IA chaperone, responsible for the binding of BteA's N-terminal domain. We bring forth extensive evidence that BtcA binds its substrate effector through a dual-interface binding mechanism comprising of non-globular and bi-globular interactions at a moderate micromolar level binding affinity. We demonstrate that the non-globular interactions involve the first 31 N-terminal residues of BteA287 and their removal leads to destabilization of the effector-chaperone complex and lower binding affinities to BtcA. These findings represent an important first step towards a molecular understanding of BteA secretion and cell entry.
format	article
author	Chen Guttman Geula Davidov Adi Yahalom Hadassa Shaked Sofiya Kolusheva Ronit Bitton Shiran Barber-Zucker Jordan H Chill Raz Zarivach
author_facet	Chen Guttman Geula Davidov Adi Yahalom Hadassa Shaked Sofiya Kolusheva Ronit Bitton Shiran Barber-Zucker Jordan H Chill Raz Zarivach
author_sort	Chen Guttman
title	BtcA, A class IA type III chaperone, interacts with the BteA N-terminal domain through a globular/non-globular mechanism.
title_short	BtcA, A class IA type III chaperone, interacts with the BteA N-terminal domain through a globular/non-globular mechanism.
title_full	BtcA, A class IA type III chaperone, interacts with the BteA N-terminal domain through a globular/non-globular mechanism.
title_fullStr	BtcA, A class IA type III chaperone, interacts with the BteA N-terminal domain through a globular/non-globular mechanism.
title_full_unstemmed	BtcA, A class IA type III chaperone, interacts with the BteA N-terminal domain through a globular/non-globular mechanism.
title_sort	btca, a class ia type iii chaperone, interacts with the btea n-terminal domain through a globular/non-globular mechanism.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/170ed984def44f2d8f50b288c5223983
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BtcA, A class IA type III chaperone, interacts with the BteA N-terminal domain through a globular/non-globular mechanism.

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