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

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 vaccin...

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Autores principales: Jo, Chang Hwa, Son, Jonghyeon, Kim, Sulhee, Oda, Takashi, Kim, Jaehoon, Lee, Myoung-Ro, Sato, Mamoru, Kim, Hyun Tae, Unzai, Satoru, Park, Sam-Yong, Hwang, Kwang Yeon
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5431922/
https://www.ncbi.nlm.nih.gov/pubmed/28496122
http://dx.doi.org/10.1038/s41598-017-02044-0
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author Jo, Chang Hwa
Son, Jonghyeon
Kim, Sulhee
Oda, Takashi
Kim, Jaehoon
Lee, Myoung-Ro
Sato, Mamoru
Kim, Hyun Tae
Unzai, Satoru
Park, Sam-Yong
Hwang, Kwang Yeon
author_facet Jo, Chang Hwa
Son, Jonghyeon
Kim, Sulhee
Oda, Takashi
Kim, Jaehoon
Lee, Myoung-Ro
Sato, Mamoru
Kim, Hyun Tae
Unzai, Satoru
Park, Sam-Yong
Hwang, Kwang Yeon
author_sort Jo, Chang Hwa
collection PubMed
description 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 Ca(2+)-binding sites (named CB1 and CB2), but Ca(2+) 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 Ca(2+) ion binding using small-angle X-ray scattering analysis and molecular dynamics simulations. The Ca(2+)-bound form has a more extended conformation than the Ca(2+)-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.
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spelling pubmed-54319222017-05-16 Structural insights into a 20.8-kDa tegumental-allergen-like (TAL) protein from Clonorchis sinensis Jo, Chang Hwa Son, Jonghyeon Kim, Sulhee Oda, Takashi Kim, Jaehoon Lee, Myoung-Ro Sato, Mamoru Kim, Hyun Tae Unzai, Satoru Park, Sam-Yong Hwang, Kwang Yeon Sci Rep Article 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 Ca(2+)-binding sites (named CB1 and CB2), but Ca(2+) 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 Ca(2+) ion binding using small-angle X-ray scattering analysis and molecular dynamics simulations. The Ca(2+)-bound form has a more extended conformation than the Ca(2+)-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. Nature Publishing Group UK 2017-05-11 /pmc/articles/PMC5431922/ /pubmed/28496122 http://dx.doi.org/10.1038/s41598-017-02044-0 Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Jo, Chang Hwa
Son, Jonghyeon
Kim, Sulhee
Oda, Takashi
Kim, Jaehoon
Lee, Myoung-Ro
Sato, Mamoru
Kim, Hyun Tae
Unzai, Satoru
Park, Sam-Yong
Hwang, Kwang Yeon
Structural insights into a 20.8-kDa tegumental-allergen-like (TAL) protein from Clonorchis sinensis
title 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_short 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
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5431922/
https://www.ncbi.nlm.nih.gov/pubmed/28496122
http://dx.doi.org/10.1038/s41598-017-02044-0
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