Comparative analyses and structural insights of new class glutathione transferases in Cryptosporidium species

Abstract Cryptosporidiosis, caused by protozoan parasites of the genus Cryptosporidium, is estimated to rank as a leading cause in the global burden of neglected zoonotic parasitic diseases. This diarrheal disease is the second leading cause of death in children under 5 years of age. Based on the C....

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Autores principales:	Mbalenhle Sizamile Mfeka, José Martínez-Oyanedel, Wanping Chen, Ikechukwu Achilonu, Khajamohiddin Syed, Thandeka Khoza
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/2bdd449fc27a4330a1176543b3ed36ba
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spelling	oai:doaj.org-article:2bdd449fc27a4330a1176543b3ed36ba2021-12-02T12:33:45ZComparative analyses and structural insights of new class glutathione transferases in Cryptosporidium species10.1038/s41598-020-77233-52045-2322https://doaj.org/article/2bdd449fc27a4330a1176543b3ed36ba2020-11-01T00:00:00Zhttps://doi.org/10.1038/s41598-020-77233-5https://doaj.org/toc/2045-2322Abstract Cryptosporidiosis, caused by protozoan parasites of the genus Cryptosporidium, is estimated to rank as a leading cause in the global burden of neglected zoonotic parasitic diseases. This diarrheal disease is the second leading cause of death in children under 5 years of age. Based on the C. parvum transcriptome data, glutathione transferase (GST) has been suggested as a drug target against this pathogen. GSTs are diverse multifunctional proteins involved in cellular defense and detoxification in organisms and help pathogens to alleviate chemical and environmental stress. In this study, we performed genome-wide data mining, identification, classification and in silico structural analysis of GSTs in fifteen Cryptosporidium species. The study revealed the presence three GSTs in each of the Cryptosporidium species analyzed in the study. Based on the percentage identity and comprehensive comparative phylogenetic analysis, we assigned Cryptosporidium species GSTs to three new GST classes, named Vega (ϑ), Gamma (γ) and Psi (ψ). The study also revealed an atypical thioredoxin-like fold in the C. parvum GST1 of the Vega class, whereas C. parvum GST2 of the Gamma class and C. melagridis GST3 of the Psi class has a typical thioredoxin-like fold in the N-terminal region. This study reports the first comparative analysis of GSTs in Cryptosporidium species.Mbalenhle Sizamile MfekaJosé Martínez-OyanedelWanping ChenIkechukwu AchilonuKhajamohiddin SyedThandeka KhozaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 10, Iss 1, Pp 1-12 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Mbalenhle Sizamile Mfeka José Martínez-Oyanedel Wanping Chen Ikechukwu Achilonu Khajamohiddin Syed Thandeka Khoza Comparative analyses and structural insights of new class glutathione transferases in Cryptosporidium species
description	Abstract Cryptosporidiosis, caused by protozoan parasites of the genus Cryptosporidium, is estimated to rank as a leading cause in the global burden of neglected zoonotic parasitic diseases. This diarrheal disease is the second leading cause of death in children under 5 years of age. Based on the C. parvum transcriptome data, glutathione transferase (GST) has been suggested as a drug target against this pathogen. GSTs are diverse multifunctional proteins involved in cellular defense and detoxification in organisms and help pathogens to alleviate chemical and environmental stress. In this study, we performed genome-wide data mining, identification, classification and in silico structural analysis of GSTs in fifteen Cryptosporidium species. The study revealed the presence three GSTs in each of the Cryptosporidium species analyzed in the study. Based on the percentage identity and comprehensive comparative phylogenetic analysis, we assigned Cryptosporidium species GSTs to three new GST classes, named Vega (ϑ), Gamma (γ) and Psi (ψ). The study also revealed an atypical thioredoxin-like fold in the C. parvum GST1 of the Vega class, whereas C. parvum GST2 of the Gamma class and C. melagridis GST3 of the Psi class has a typical thioredoxin-like fold in the N-terminal region. This study reports the first comparative analysis of GSTs in Cryptosporidium species.
format	article
author	Mbalenhle Sizamile Mfeka José Martínez-Oyanedel Wanping Chen Ikechukwu Achilonu Khajamohiddin Syed Thandeka Khoza
author_facet	Mbalenhle Sizamile Mfeka José Martínez-Oyanedel Wanping Chen Ikechukwu Achilonu Khajamohiddin Syed Thandeka Khoza
author_sort	Mbalenhle Sizamile Mfeka
title	Comparative analyses and structural insights of new class glutathione transferases in Cryptosporidium species
title_short	Comparative analyses and structural insights of new class glutathione transferases in Cryptosporidium species
title_full	Comparative analyses and structural insights of new class glutathione transferases in Cryptosporidium species
title_fullStr	Comparative analyses and structural insights of new class glutathione transferases in Cryptosporidium species
title_full_unstemmed	Comparative analyses and structural insights of new class glutathione transferases in Cryptosporidium species
title_sort	comparative analyses and structural insights of new class glutathione transferases in cryptosporidium species
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/2bdd449fc27a4330a1176543b3ed36ba
work_keys_str_mv	AT mbalenhlesizamilemfeka comparativeanalysesandstructuralinsightsofnewclassglutathionetransferasesincryptosporidiumspecies AT josemartinezoyanedel comparativeanalysesandstructuralinsightsofnewclassglutathionetransferasesincryptosporidiumspecies AT wanpingchen comparativeanalysesandstructuralinsightsofnewclassglutathionetransferasesincryptosporidiumspecies AT ikechukwuachilonu comparativeanalysesandstructuralinsightsofnewclassglutathionetransferasesincryptosporidiumspecies AT khajamohiddinsyed comparativeanalysesandstructuralinsightsofnewclassglutathionetransferasesincryptosporidiumspecies AT thandekakhoza comparativeanalysesandstructuralinsightsofnewclassglutathionetransferasesincryptosporidiumspecies
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Comparative analyses and structural insights of new class glutathione transferases in Cryptosporidium species

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