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Molecular characterisation and expression analysis of two heat-shock proteins in Taenia multiceps
BACKGROUND: Taenia multiceps is a harmful tapeworm and its larval form (coenurus cerebralis) is the causative agent of coenurosis, a disease affecting the health of herbivores, resulting in great economic loss to animal husbandry. Heat-shock proteins (HSPs), expressed in all prokaryotes and eukaryot...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6417115/ https://www.ncbi.nlm.nih.gov/pubmed/30867020 http://dx.doi.org/10.1186/s13071-019-3352-8 |
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author | Liu, Yuchen Guo, Cheng Dong, Xiaowei Gu, Xiaobin Xie, Yue Lai, Weimin Peng, Xuerong Yang, Guangyou |
author_facet | Liu, Yuchen Guo, Cheng Dong, Xiaowei Gu, Xiaobin Xie, Yue Lai, Weimin Peng, Xuerong Yang, Guangyou |
author_sort | Liu, Yuchen |
collection | PubMed |
description | BACKGROUND: Taenia multiceps is a harmful tapeworm and its larval form (coenurus cerebralis) is the causative agent of coenurosis, a disease affecting the health of herbivores, resulting in great economic loss to animal husbandry. Heat-shock proteins (HSPs), expressed in all prokaryotes and eukaryotes, act as molecular chaperones and can affect pathogenicity. METHODS: Herein, cDNAs of T. multiceps genes Tm-HSP60 and Tm-p36 were cloned and molecularly characterised by bioinformatics analyses. The immunogenicity and immunoreactivity of recombinant rTm-HSP60 and rTm-p36 proteins were investigated by immunoblotting and indirect ELISA was established to evaluate their serodiagnostic potential. Tissue localisation and transcriptional level at different life stages of T. multiceps were determined by immunohistochemical and quantitative real-time PCR analyses. RESULT: The 533 residue rTm-HSP60 and the 314 residue rTm-p36 proteins share typical highly conserved features of HSPs. Tm-p36 shares structural characteristics with metazoan small HSPs, with two N-terminal α-crystallin domains. Compared with Tm-p36, Tm-HSP60 displayed stronger immunogenicity, and the indirect ELISA based on rTm-HSP60 exhibited a sensitivity of 83.3% and a specificity of 87.5%, while rTm-p36 was not suitable to develop indirect ELISA. Tm-HSP60 was widely distributed in all stages of T. multiceps, albeit at relatively low levels, while Tm-p36 was specifically distributed in the protoscolex and oncosphere. CONCLUSIONS: The sequence, structural and functional analyses of these two HSPs indicates that they may play important roles in the life-cycle of T. multiceps as molecular chaperones. Tm-HSP60 displayed stronger immunogenicity compare to Tm-p36, and has the potential for antibody detection. Tm-p36 was strongly associated with the activation of oncospheres and has potential interest for vaccination. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s13071-019-3352-8) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-6417115 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-64171152019-03-25 Molecular characterisation and expression analysis of two heat-shock proteins in Taenia multiceps Liu, Yuchen Guo, Cheng Dong, Xiaowei Gu, Xiaobin Xie, Yue Lai, Weimin Peng, Xuerong Yang, Guangyou Parasit Vectors Research BACKGROUND: Taenia multiceps is a harmful tapeworm and its larval form (coenurus cerebralis) is the causative agent of coenurosis, a disease affecting the health of herbivores, resulting in great economic loss to animal husbandry. Heat-shock proteins (HSPs), expressed in all prokaryotes and eukaryotes, act as molecular chaperones and can affect pathogenicity. METHODS: Herein, cDNAs of T. multiceps genes Tm-HSP60 and Tm-p36 were cloned and molecularly characterised by bioinformatics analyses. The immunogenicity and immunoreactivity of recombinant rTm-HSP60 and rTm-p36 proteins were investigated by immunoblotting and indirect ELISA was established to evaluate their serodiagnostic potential. Tissue localisation and transcriptional level at different life stages of T. multiceps were determined by immunohistochemical and quantitative real-time PCR analyses. RESULT: The 533 residue rTm-HSP60 and the 314 residue rTm-p36 proteins share typical highly conserved features of HSPs. Tm-p36 shares structural characteristics with metazoan small HSPs, with two N-terminal α-crystallin domains. Compared with Tm-p36, Tm-HSP60 displayed stronger immunogenicity, and the indirect ELISA based on rTm-HSP60 exhibited a sensitivity of 83.3% and a specificity of 87.5%, while rTm-p36 was not suitable to develop indirect ELISA. Tm-HSP60 was widely distributed in all stages of T. multiceps, albeit at relatively low levels, while Tm-p36 was specifically distributed in the protoscolex and oncosphere. CONCLUSIONS: The sequence, structural and functional analyses of these two HSPs indicates that they may play important roles in the life-cycle of T. multiceps as molecular chaperones. Tm-HSP60 displayed stronger immunogenicity compare to Tm-p36, and has the potential for antibody detection. Tm-p36 was strongly associated with the activation of oncospheres and has potential interest for vaccination. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s13071-019-3352-8) contains supplementary material, which is available to authorized users. BioMed Central 2019-03-12 /pmc/articles/PMC6417115/ /pubmed/30867020 http://dx.doi.org/10.1186/s13071-019-3352-8 Text en © The Author(s) 2019 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Liu, Yuchen Guo, Cheng Dong, Xiaowei Gu, Xiaobin Xie, Yue Lai, Weimin Peng, Xuerong Yang, Guangyou Molecular characterisation and expression analysis of two heat-shock proteins in Taenia multiceps |
title | Molecular characterisation and expression analysis of two heat-shock proteins in Taenia multiceps |
title_full | Molecular characterisation and expression analysis of two heat-shock proteins in Taenia multiceps |
title_fullStr | Molecular characterisation and expression analysis of two heat-shock proteins in Taenia multiceps |
title_full_unstemmed | Molecular characterisation and expression analysis of two heat-shock proteins in Taenia multiceps |
title_short | Molecular characterisation and expression analysis of two heat-shock proteins in Taenia multiceps |
title_sort | molecular characterisation and expression analysis of two heat-shock proteins in taenia multiceps |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6417115/ https://www.ncbi.nlm.nih.gov/pubmed/30867020 http://dx.doi.org/10.1186/s13071-019-3352-8 |
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