Objective: To investigate the immune response and the protection in mice induced by the recombinant myophilin protein of Echinococcus granulosus.
Methods: Thirty-six male ICR mice of 6-8 weeks old were randomly divided into groups A, B and C each with 12. The mice in the 3 groups were subcutaneously immunized with Eg myophilin protein, blank plasmid protein or PBS, respectively, by 3 times and challenged with protoscoleces of E. granulosus 2wk after the last vaccination. Mice were sacrificed 20wk after the infection, the hydatid cysts were collected for measuring the weight reduction. Spleens were obtained and the splenocytes were separated and cultured in vitro with EgAg or ConA stimulus for 4-5 h. The subsets of CD4+ and CD8+ T cells were measured by FACsort. The proliferation of splenocytes was determined by MTT method with blank plasmid and PBS as control.
Results: The average weight of the hydatid cysts in the immunized group decreased by 69.1% in comparison to the blank plasmid and PBS groups. The CD4+ subset [(29.7 +/- 0.9)%] and CD84+ subset [(9.7 +/- 0.8)%] in group A increased significantly than group C, [(11.6 +/- 1.4)%] and [(7.8 +/- 0.2)%] respectively (P < 0.01 or < 0.05). The ratio of CD4+/CD8+ subsets in group A (3.061 +/- 0.015) was also higher than group C (1.487 +/- 0.106) (P < 0.01). Without stimulation, the proliferation of T lymphocytes in group A(0.237 +/- 0.009) was higher than group C (0.159 +/- 0.005) (P < 0.01), with EgAg or ConA stimulus, it was also higher in group A than that of group C (P < 0.01).
Conclusion: The recombinant myophilin protein of E. granulosus can induce the proliferation of splenocytes and Th1 response in mice, and the CD4+ T cells subset may bear a part in the induced protection against the challenge of protoscoleces.
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Exp Ther Med
September 2016
Center of Scientific Technology, Ningxia Medical University, Yinchuan, Ningxia 750004, P.R. China; Key Laboratory of Hydatid Disease, Ningxia Medical University, Yinchuan, Ningxia 750004, P.R. China.
The aims of the present study were to investigate the immunoprotection of recombinant myophilin (rEg.myophilin) against the establishment of a challenge oral infection with eggs, as well as to determine the mechanisms underlying this protection. Sheep were subcutaneously immunized two times with rEg.
View Article and Find Full Text PDFZhongguo Ji Sheng Chong Xue Yu Ji Sheng Chong Bing Za Zhi
October 2012
Higher Health Vocational and Technical College of Ningxia Medical University, Yinchuan 750004, China.
Objective: To investigate the immune response and the protection in mice induced by the recombinant myophilin protein of Echinococcus granulosus.
Methods: Thirty-six male ICR mice of 6-8 weeks old were randomly divided into groups A, B and C each with 12. The mice in the 3 groups were subcutaneously immunized with Eg myophilin protein, blank plasmid protein or PBS, respectively, by 3 times and challenged with protoscoleces of E.
Parasitol Res
September 2012
Department of Parasitology, Zhongshan School of Medicine, Sun Yat-Sen University, Guangzhou, 510080, China.
Clonorchiasis, caused by Clonorchis sinensis infection, has been an important public health problem in China. More messages about biology and pathogenicity of C. sinensis will be better for development of new strategies for clonorchiasis control.
View Article and Find Full Text PDFVet Res Commun
April 2011
Medical Molecular Biology Laboratory, Ningxia Medical University, Yinchuan, Ningxia Hui Autonomous Region 750004, China.
Objects: This study aimed to investigate the immunoprotection of the recombinant Eg.myophilin (rEg.myophilin) and tentatively analyze mechanism of this protection.
View Article and Find Full Text PDFExp Parasitol
May 2008
Shanghai Institute of Hematology, Ruijin Hospital, State Key Laboratory of Medical Genomics, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
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.
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