Identification and functional analysis of cadmium-binding protein in the visceral mass of Crassostrea gigas

Abstract The Pacific oyster, Crassostrea gigas, is a traditional food worldwide. The soft body of the oyster can easily accumulate heavy metals such as cadmium (Cd). To clarify the molecular mechanism of Cd accumulation in the viscera of C. gigas, we identified Cd-binding proteins. 5,10,15,20-Tetrap...

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Autores principales:	Zehua Zheng, Kazuhiro Kawakami, Dingkun Zhang, Lumi Negishi, Mohamed Abomosallam, Tomiko Asakura, Koji Nagata, Michio Suzuki
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/983c6b04f0784e28b3e6a1135551ce95
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spelling	oai:doaj.org-article:983c6b04f0784e28b3e6a1135551ce952021-12-02T14:49:24ZIdentification and functional analysis of cadmium-binding protein in the visceral mass of Crassostrea gigas10.1038/s41598-021-90882-42045-2322https://doaj.org/article/983c6b04f0784e28b3e6a1135551ce952021-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-90882-4https://doaj.org/toc/2045-2322Abstract The Pacific oyster, Crassostrea gigas, is a traditional food worldwide. The soft body of the oyster can easily accumulate heavy metals such as cadmium (Cd). To clarify the molecular mechanism of Cd accumulation in the viscera of C. gigas, we identified Cd-binding proteins. 5,10,15,20-Tetraphenyl-21H,23H-porphinetetrasulfonic acid, disulfuric acid, tetrahydrate, and Cd-binding competition experiments using immobilized metal ion affinity chromatography revealed the binding of water-soluble high molecular weight proteins to Cd, including C. gigas protein disulfide isomerase (cgPDI). Liquid chromatography–tandem mass spectrometry (LC–MS/MS) analyses revealed two CGHC motifs in cgPDI. The binding between Cd and rcgPDI was confirmed through a Cd-binding experiment using the TPPS method. Isothermal titration calorimetry (ITC) revealed the binding of two Cd ions to one molecule of rcgPDI. Circular dichroism (CD) spectrum and tryptophan fluorescence analyses demonstrated that the rcgPDI bound to Cd. The binding markedly changed the two-dimensional or three-dimensional structures. The activity of rcgPDI measured by a PDI Activity Assay Kit was more affected by the addition of Cd than by human PDI. Immunological analyses indicated that C. gigas contained cgPDI at a concentration of 1.0 nmol/g (viscera wet weight). The combination of ITC and quantification results revealed that Cd-binding to cgPDI accounted for 20% of the total bound Cd in the visceral mass. The findings provide new insights into the defense mechanisms of invertebrates against Cd.Zehua ZhengKazuhiro KawakamiDingkun ZhangLumi NegishiMohamed AbomosallamTomiko AsakuraKoji NagataMichio SuzukiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Zehua Zheng Kazuhiro Kawakami Dingkun Zhang Lumi Negishi Mohamed Abomosallam Tomiko Asakura Koji Nagata Michio Suzuki Identification and functional analysis of cadmium-binding protein in the visceral mass of Crassostrea gigas
description	Abstract The Pacific oyster, Crassostrea gigas, is a traditional food worldwide. The soft body of the oyster can easily accumulate heavy metals such as cadmium (Cd). To clarify the molecular mechanism of Cd accumulation in the viscera of C. gigas, we identified Cd-binding proteins. 5,10,15,20-Tetraphenyl-21H,23H-porphinetetrasulfonic acid, disulfuric acid, tetrahydrate, and Cd-binding competition experiments using immobilized metal ion affinity chromatography revealed the binding of water-soluble high molecular weight proteins to Cd, including C. gigas protein disulfide isomerase (cgPDI). Liquid chromatography–tandem mass spectrometry (LC–MS/MS) analyses revealed two CGHC motifs in cgPDI. The binding between Cd and rcgPDI was confirmed through a Cd-binding experiment using the TPPS method. Isothermal titration calorimetry (ITC) revealed the binding of two Cd ions to one molecule of rcgPDI. Circular dichroism (CD) spectrum and tryptophan fluorescence analyses demonstrated that the rcgPDI bound to Cd. The binding markedly changed the two-dimensional or three-dimensional structures. The activity of rcgPDI measured by a PDI Activity Assay Kit was more affected by the addition of Cd than by human PDI. Immunological analyses indicated that C. gigas contained cgPDI at a concentration of 1.0 nmol/g (viscera wet weight). The combination of ITC and quantification results revealed that Cd-binding to cgPDI accounted for 20% of the total bound Cd in the visceral mass. The findings provide new insights into the defense mechanisms of invertebrates against Cd.
format	article
author	Zehua Zheng Kazuhiro Kawakami Dingkun Zhang Lumi Negishi Mohamed Abomosallam Tomiko Asakura Koji Nagata Michio Suzuki
author_facet	Zehua Zheng Kazuhiro Kawakami Dingkun Zhang Lumi Negishi Mohamed Abomosallam Tomiko Asakura Koji Nagata Michio Suzuki
author_sort	Zehua Zheng
title	Identification and functional analysis of cadmium-binding protein in the visceral mass of Crassostrea gigas
title_short	Identification and functional analysis of cadmium-binding protein in the visceral mass of Crassostrea gigas
title_full	Identification and functional analysis of cadmium-binding protein in the visceral mass of Crassostrea gigas
title_fullStr	Identification and functional analysis of cadmium-binding protein in the visceral mass of Crassostrea gigas
title_full_unstemmed	Identification and functional analysis of cadmium-binding protein in the visceral mass of Crassostrea gigas
title_sort	identification and functional analysis of cadmium-binding protein in the visceral mass of crassostrea gigas
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/983c6b04f0784e28b3e6a1135551ce95
work_keys_str_mv	AT zehuazheng identificationandfunctionalanalysisofcadmiumbindingproteininthevisceralmassofcrassostreagigas AT kazuhirokawakami identificationandfunctionalanalysisofcadmiumbindingproteininthevisceralmassofcrassostreagigas AT dingkunzhang identificationandfunctionalanalysisofcadmiumbindingproteininthevisceralmassofcrassostreagigas AT luminegishi identificationandfunctionalanalysisofcadmiumbindingproteininthevisceralmassofcrassostreagigas AT mohamedabomosallam identificationandfunctionalanalysisofcadmiumbindingproteininthevisceralmassofcrassostreagigas AT tomikoasakura identificationandfunctionalanalysisofcadmiumbindingproteininthevisceralmassofcrassostreagigas AT kojinagata identificationandfunctionalanalysisofcadmiumbindingproteininthevisceralmassofcrassostreagigas AT michiosuzuki identificationandfunctionalanalysisofcadmiumbindingproteininthevisceralmassofcrassostreagigas
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Identification and functional analysis of cadmium-binding protein in the visceral mass of Crassostrea gigas

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