Structural Analysis of an Epitope Candidate of Triosephosphate Isomerase in Opisthorchis viverrini

Abstract Opisthorchis viverrini, a parasitic trematode, was recategorized as a group 1 biological carcinogen because it causes opisthorchiasis, which may result in cholangiocarcinoma. A new strategy for controlling opisthorchiasis is needed because of issues such as drug resistance and reinfection....

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Jonghyeon Son, Sulhee Kim, So Eun Kim, Haemin Lee, Myoung-Ro Lee, Kwang Yeon Hwang
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Opisthorchis Viverrini Triosephosphate Isomerase Local Structural Alterations Unique Tripeptide Biological Carcinogens Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f088385d49604a9ebf9330ce91937de2
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:f088385d49604a9ebf9330ce91937de2
record_format	dspace
spelling	oai:doaj.org-article:f088385d49604a9ebf9330ce91937de22021-12-02T15:08:18ZStructural Analysis of an Epitope Candidate of Triosephosphate Isomerase in Opisthorchis viverrini10.1038/s41598-018-33479-82045-2322https://doaj.org/article/f088385d49604a9ebf9330ce91937de22018-10-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-33479-8https://doaj.org/toc/2045-2322Abstract Opisthorchis viverrini, a parasitic trematode, was recategorized as a group 1 biological carcinogen because it causes opisthorchiasis, which may result in cholangiocarcinoma. A new strategy for controlling opisthorchiasis is needed because of issues such as drug resistance and reinfection. Triosephosphate isomerase (TIM), a key enzyme in energy metabolism, is regarded as a potential drug target and vaccine candidate against various pathogens. Here, we determined the crystal structures of wild-type and 3 variants of TIMs from O. viverrini (OvTIM) at high resolution. The unique tripeptide of parasite trematodes, the SAD motif, was located on the surface of OvTIM and contributed to forming a 310-helix of the following loop in a sequence-independent manner. Through thermal stability and structural analyses of OvTIM variants, we found that the SAD motif induced local structural alterations of the surface and was involved in the overall stability of OvTIM in a complementary manner with another parasite-specific residue, N115. Comparison of the surface characteristics between OvTIM and Homo sapiens TIM (HsTIM) and structure-based epitope prediction suggested that the SAD motif functions as an epitope.Jonghyeon SonSulhee KimSo Eun KimHaemin LeeMyoung-Ro LeeKwang Yeon HwangNature PortfolioarticleOpisthorchis ViverriniTriosephosphate IsomeraseLocal Structural AlterationsUnique TripeptideBiological CarcinogensMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-10 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Opisthorchis Viverrini Triosephosphate Isomerase Local Structural Alterations Unique Tripeptide Biological Carcinogens Medicine R Science Q
spellingShingle	Opisthorchis Viverrini Triosephosphate Isomerase Local Structural Alterations Unique Tripeptide Biological Carcinogens Medicine R Science Q Jonghyeon Son Sulhee Kim So Eun Kim Haemin Lee Myoung-Ro Lee Kwang Yeon Hwang Structural Analysis of an Epitope Candidate of Triosephosphate Isomerase in Opisthorchis viverrini
description	Abstract Opisthorchis viverrini, a parasitic trematode, was recategorized as a group 1 biological carcinogen because it causes opisthorchiasis, which may result in cholangiocarcinoma. A new strategy for controlling opisthorchiasis is needed because of issues such as drug resistance and reinfection. Triosephosphate isomerase (TIM), a key enzyme in energy metabolism, is regarded as a potential drug target and vaccine candidate against various pathogens. Here, we determined the crystal structures of wild-type and 3 variants of TIMs from O. viverrini (OvTIM) at high resolution. The unique tripeptide of parasite trematodes, the SAD motif, was located on the surface of OvTIM and contributed to forming a 310-helix of the following loop in a sequence-independent manner. Through thermal stability and structural analyses of OvTIM variants, we found that the SAD motif induced local structural alterations of the surface and was involved in the overall stability of OvTIM in a complementary manner with another parasite-specific residue, N115. Comparison of the surface characteristics between OvTIM and Homo sapiens TIM (HsTIM) and structure-based epitope prediction suggested that the SAD motif functions as an epitope.
format	article
author	Jonghyeon Son Sulhee Kim So Eun Kim Haemin Lee Myoung-Ro Lee Kwang Yeon Hwang
author_facet	Jonghyeon Son Sulhee Kim So Eun Kim Haemin Lee Myoung-Ro Lee Kwang Yeon Hwang
author_sort	Jonghyeon Son
title	Structural Analysis of an Epitope Candidate of Triosephosphate Isomerase in Opisthorchis viverrini
title_short	Structural Analysis of an Epitope Candidate of Triosephosphate Isomerase in Opisthorchis viverrini
title_full	Structural Analysis of an Epitope Candidate of Triosephosphate Isomerase in Opisthorchis viverrini
title_fullStr	Structural Analysis of an Epitope Candidate of Triosephosphate Isomerase in Opisthorchis viverrini
title_full_unstemmed	Structural Analysis of an Epitope Candidate of Triosephosphate Isomerase in Opisthorchis viverrini
title_sort	structural analysis of an epitope candidate of triosephosphate isomerase in opisthorchis viverrini
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/f088385d49604a9ebf9330ce91937de2
work_keys_str_mv	AT jonghyeonson structuralanalysisofanepitopecandidateoftriosephosphateisomeraseinopisthorchisviverrini AT sulheekim structuralanalysisofanepitopecandidateoftriosephosphateisomeraseinopisthorchisviverrini AT soeunkim structuralanalysisofanepitopecandidateoftriosephosphateisomeraseinopisthorchisviverrini AT haeminlee structuralanalysisofanepitopecandidateoftriosephosphateisomeraseinopisthorchisviverrini AT myoungrolee structuralanalysisofanepitopecandidateoftriosephosphateisomeraseinopisthorchisviverrini AT kwangyeonhwang structuralanalysisofanepitopecandidateoftriosephosphateisomeraseinopisthorchisviverrini
_version_	1718388226621702144

Structural Analysis of an Epitope Candidate of Triosephosphate Isomerase in Opisthorchis viverrini

Ejemplares similares