Molecular characterisation and expression analysis of two heat-shock proteins in Taenia multiceps.

Authors:
Yuchen Liu
Yuchen Liu
Peking University Shenzhen Hospital
China
Cheng Guo
Cheng Guo
Shanghai Jiao Tong University Affiliated Sixth People's Hospital
China
Xiaowei Dong
Xiaowei Dong
University of Kentucky
United States
Xiaobin Gu
Xiaobin Gu
Sichuan Agricultural University
China
Yue Xie
Yue Xie
Sichuan Agricultural University
China
Weimin Lai
Weimin Lai
Sichuan Agricultural University
China
Xuerong Peng
Xuerong Peng
Sichuan Agricultural University
China
Guangyou Yang
Guangyou Yang
College of Veterinary Medicine
China

Parasit Vectors 2019 Mar 12;12(1):93. Epub 2019 Mar 12.

Department of Parasitology, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang, 611130, China.

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.

Download full-text PDF

Source
http://dx.doi.org/10.1186/s13071-019-3352-8DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6417115PMC

Still can't find the full text of the article?

We can help you send a request to the authors directly.
March 2019
3 Reads

Publication Analysis

Top Keywords

indirect elisa
12
taenia multiceps
8
stages multiceps
8
tm-hsp60 displayed
8
molecular chaperones
8
heat-shock proteins
8
stronger immunogenicity
8
rtm-p36 proteins
8
displayed stronger
8
tm-p36
6
multiceps
6
tm-p36 shares
4
highly conserved
4
typical highly
4
hsps tm-p36
4
features hsps
4
share typical
4
shares structural
4
conserved features
4
small hsps
4

References

(Supplied by CrossRef)
Article in Parasit Vectors.
H Xing et al.
Parasit Vectors. 2015
Article in Res Vet Sci.
WH Li et al.
Res Vet Sci. 2015
Article in J Zoo Wildl Med.
Y Merbl et al.
J Zoo Wildl Med. 2014
Article in Vet Parasitol.
N Wang et al.
Vet Parasitol. 2018
Article in Parasit Vectors.
H Xing et al.
Parasit Vectors. 2016
Article in Parasitol Res.
M Dehghani et al.
Parasitol Res. 2016
Article in Parasitol Res.
G Cheng et al.
Parasitol Res. 2017
Article in JAMA.
JA Hermos et al.
JAMA. 1970
Article in Parasitol Res.
HM Nie et al.
Parasitol Res. 2013
Article in DNA Res.
W Li et al.
DNA Res. 2018
Article in Parasitol Today.
B Maresca et al.
Parasitol Today. 1992

Similar Publications