Expression, immunolocalization and serodiagnostic value of a myophilin-like protein from Schistosoma japonicum.

Abstract:

:The cDNA of a Schistosoma japonicum myophilin-like protein was cloned, sequenced, and expressed in Escherichia coli as a recombined protein (rSj myophilin-like protein), and the protein was purified by affinity chromatography. The deduced amino acid sequences of the Sj myophilin-like protein showed significant homology to myophilin, calponin, Np22 and Mp20. Northern blot and RT-PCR analyzes revealed expression of the Sj myophilin-like protein mRNA in eggs, sporocysts, cercariae, hepatic schistosomula and adult worms. Confocal fluorescence microscopy localized the native protein to the muscle of the adult worm. In schistosome-infected rabbits, the rSj myophilin-like protein antibody level, assessed by ELISA, was elevated after infection but was reduced after praziquantel treatment. In humans, the myophilin-like protein antibody level was evaluated by ELISA in sera from 33 non-infected humans and 61 schistosomiasis patients; the results showed a highly significant difference between the two groups with a sensitivity of 57.4%. Taken together, the myophilin-like protein may prove useful for monitoring the therapeutic effect of praziquantel rather than in serodiagnosis of schistosomiasis.

journal_name

Exp Parasitol

authors

Peng H,Song K,Huang C,Ye S,Song H,Hu W,Han Z,McManus DP,Zhao G,Zhang Q

doi

10.1016/j.exppara.2008.01.017

subject

Has Abstract

pub_date

2008-05-01 00:00:00

pages

117-24

issue

1

eissn

0014-4894

issn

1090-2449

pii

S0014-4894(08)00035-0

journal_volume

119

pub_type

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