Functional characterisation of Schistosoma japonicum acetylcholinesterase

You, Hong, Gobert, Geoffrey N., Du, Xiaofeng, Pali, Gabor, Cai, Pengfei, Jones, Malcolm K. and McManus, Donald P. (2016) Functional characterisation of Schistosoma japonicum acetylcholinesterase. Parasites & Vectors, 9 . doi:10.1186/s13071-016-1615-1


Author You, Hong
Gobert, Geoffrey N.
Du, Xiaofeng
Pali, Gabor
Cai, Pengfei
Jones, Malcolm K.
McManus, Donald P.
Title Functional characterisation of Schistosoma japonicum acetylcholinesterase
Formatted title
Functional characterisation of Schistosoma japonicum acetylcholinesterase
Journal name Parasites & Vectors   Check publisher's open access policy
ISSN 1756-3305
Publication date 2016-06-10
Year available 2016
Sub-type Article (original research)
DOI 10.1186/s13071-016-1615-1
Open Access Status DOI
Volume 9
Total pages 12
Place of publication London, United Kingdom
Publisher BioMed Central
Collection year 2017
Language eng
Formatted abstract
Background: Acetylcholinesterase (AChE) is an important metabolic enzyme of schistosomes present in the musculature and on the surface of the blood stage where it has been implicated in the modulation of glucose scavenging from mammalian host blood. As both a target for the antischistosomal drug metrifonate and as a potential vaccine candidate, AChE has been characterised in the schistosome species Schistosoma mansoni, S. haematobium and S. bovis, but not in S. japonicum. Recently, using a schistosome protein microarray, a predicted S. japonicum acetylcholinesterase precursor was significantly targeted by protective IgG1 immune responses in S. haematobium-exposed individuals that had acquired drug-induced resistance to schistosomiasis after praziquantel treatment.

Results: We report the full-length cDNA sequence and describe phylogenetic and molecular structural analysis to facilitate understanding of the biological function of AChE (SjAChE) in S. japonicum. The protein has high sequence identity (88 %) with the AChEs in S. mansoni, S. haematobium and S. bovis and has 25 % sequence similarity with human AChE, suggestive of a highly specialised role for the enzyme in both parasite and host. We immunolocalized SjAChE and demonstrated its presence on the surface of adult worms and schistosomula, as well as its lower expression in parenchymal regions. The relatively abundance of AChE activity (90 %) present on the surface of adult S. japonicum when compared with that reported in other schistosomes suggests SjAChE may be a more effective drug or immunological target against this species. We also demonstrate that the classical inhibitor of AChE, BW285c51, inhibited AChE activity in tegumental extracts of paired worms, single males and single females by 59, 22 and 50 %, respectively, after 24 h incubation with 200 μM BW284c51.

Conclusions: These results build on previous studies in other schistosome species indicating major differences in the enzyme between parasite and mammalian host, and provide further support for the design of an anti-schistosome intervention targeting AChE
Keyword Schistosoma japonicum
Acetylcholinesterase
Drug or vaccine target
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
School of Veterinary Science Publications
 
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