Abstract
BackgroundTaenia 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.MethodsHerein, 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.ResultThe 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.ConclusionsThe 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.
Highlights
Taenia multiceps is a harmful tapeworm and its larval form is the causative agent of coenurosis, a disease affecting the health of herbivores, resulting in great economic loss to animal husbandry
Tm-HSP60 displayed stronger immunogenicity compare to Tm-p36, and has the potential for antibody detection
Primers The cDNA sequences of Tm-HSP60 and Tm-p36 were amplified using primers designed from Unigene 5021 and 18510 of the assembled T. multiceps transcriptome dataset, which is homologous to the genome sequences of Echinococcus multilocularis (GenBank: CDS35950.1) and T. saginata (GenBank: Q7YZT0.1)
Summary
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. Taenia multiceps is a common taeniid cestode and multi-host parasite. Adult worms adhere to the small intestine of canids, while the larval stage (coenurus cerebralis) causes coenurosis, a disease affecting herbivores, Taenia multiceps has a complex life-cycle that involves different phases of development and migration within the host [9, 10]. One mechanism counteracts stress via the expression of heat-shock proteins (HSPs) that act as important molecular chaperones [11]. In addition to facilitating cytoprotection against stress, HSPs participate in the differentiation and development of parasites, and may even serve as diagnostic or vaccine candidates [12]
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