Structural insights into a 20.8-kDa tegumental-allergen-like (TAL) protein from Clonorchis sinensis

Abstract Survival of Clonorchis sinensis, a cause of human clonorchiasis, requires tegument proteins, which are localized to the tegumental outer surface membrane. These proteins play an important role in a host response and parasite survival. Thus, these proteins are interesting molecular targets f...

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Autores principales:	Chang Hwa Jo, Jonghyeon Son, Sulhee Kim, Takashi Oda, Jaehoon Kim, Myoung-Ro Lee, Mamoru Sato, Hyun Tae Kim, Satoru Unzai, Sam-Yong Park, Kwang Yeon Hwang
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ec0c4a69de244a8481135b1fe62b30fe
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spelling	oai:doaj.org-article:ec0c4a69de244a8481135b1fe62b30fe2021-12-02T15:04:56ZStructural insights into a 20.8-kDa tegumental-allergen-like (TAL) protein from Clonorchis sinensis10.1038/s41598-017-02044-02045-2322https://doaj.org/article/ec0c4a69de244a8481135b1fe62b30fe2017-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-02044-0https://doaj.org/toc/2045-2322Abstract Survival of Clonorchis sinensis, a cause of human clonorchiasis, requires tegument proteins, which are localized to the tegumental outer surface membrane. These proteins play an important role in a host response and parasite survival. Thus, these proteins are interesting molecular targets for vaccine and drug development. Here, we have determined two crystal structures of the calmodulin like domain (amino acid [aa] positions 1–81) and dynein light chain (DLC)-like domain (aa 83–177) of a 20.8-kDa tegumental-allergen-like protein from Clonorchis sinensis (CsTAL3). The calmodulin like domain has two Ca2+-binding sites (named CB1 and CB2), but Ca2+ binds to only one site, CB1. The DLC-like domain has a dimeric conformation; the interface is formed mainly by hydrogen bonds between the main chain atoms. In addition, we have determined full-length structure of CsTAL3 in solution and showed the conformational change of CsTAL3 induced by Ca2+ ion binding using small-angle X-ray scattering analysis and molecular dynamics simulations. The Ca2+-bound form has a more extended conformation than the Ca2+-free from does. These structural and biochemical analyses will advance the understanding of the biology of this liver fluke and may contribute to our understanding of the molecular mechanism of calcium-responsive and tegumental-allergen-like proteins.Chang Hwa JoJonghyeon SonSulhee KimTakashi OdaJaehoon KimMyoung-Ro LeeMamoru SatoHyun Tae KimSatoru UnzaiSam-Yong ParkKwang Yeon HwangNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Chang Hwa Jo Jonghyeon Son Sulhee Kim Takashi Oda Jaehoon Kim Myoung-Ro Lee Mamoru Sato Hyun Tae Kim Satoru Unzai Sam-Yong Park Kwang Yeon Hwang Structural insights into a 20.8-kDa tegumental-allergen-like (TAL) protein from Clonorchis sinensis
description	Abstract Survival of Clonorchis sinensis, a cause of human clonorchiasis, requires tegument proteins, which are localized to the tegumental outer surface membrane. These proteins play an important role in a host response and parasite survival. Thus, these proteins are interesting molecular targets for vaccine and drug development. Here, we have determined two crystal structures of the calmodulin like domain (amino acid [aa] positions 1–81) and dynein light chain (DLC)-like domain (aa 83–177) of a 20.8-kDa tegumental-allergen-like protein from Clonorchis sinensis (CsTAL3). The calmodulin like domain has two Ca2+-binding sites (named CB1 and CB2), but Ca2+ binds to only one site, CB1. The DLC-like domain has a dimeric conformation; the interface is formed mainly by hydrogen bonds between the main chain atoms. In addition, we have determined full-length structure of CsTAL3 in solution and showed the conformational change of CsTAL3 induced by Ca2+ ion binding using small-angle X-ray scattering analysis and molecular dynamics simulations. The Ca2+-bound form has a more extended conformation than the Ca2+-free from does. These structural and biochemical analyses will advance the understanding of the biology of this liver fluke and may contribute to our understanding of the molecular mechanism of calcium-responsive and tegumental-allergen-like proteins.
format	article
author	Chang Hwa Jo Jonghyeon Son Sulhee Kim Takashi Oda Jaehoon Kim Myoung-Ro Lee Mamoru Sato Hyun Tae Kim Satoru Unzai Sam-Yong Park Kwang Yeon Hwang
author_facet	Chang Hwa Jo Jonghyeon Son Sulhee Kim Takashi Oda Jaehoon Kim Myoung-Ro Lee Mamoru Sato Hyun Tae Kim Satoru Unzai Sam-Yong Park Kwang Yeon Hwang
author_sort	Chang Hwa Jo
title	Structural insights into a 20.8-kDa tegumental-allergen-like (TAL) protein from Clonorchis sinensis
title_short	Structural insights into a 20.8-kDa tegumental-allergen-like (TAL) protein from Clonorchis sinensis
title_full	Structural insights into a 20.8-kDa tegumental-allergen-like (TAL) protein from Clonorchis sinensis
title_fullStr	Structural insights into a 20.8-kDa tegumental-allergen-like (TAL) protein from Clonorchis sinensis
title_full_unstemmed	Structural insights into a 20.8-kDa tegumental-allergen-like (TAL) protein from Clonorchis sinensis
title_sort	structural insights into a 20.8-kda tegumental-allergen-like (tal) protein from clonorchis sinensis
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/ec0c4a69de244a8481135b1fe62b30fe
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Structural insights into a 20.8-kDa tegumental-allergen-like (TAL) protein from Clonorchis sinensis

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