A novel Schistosoma japonicum endonuclease homologous to DNase II

BMC Genomics

Qijun Chen²  Yan Xiao¹  Shuai Liu¹  Chuang Wu¹  Pengfei Cai¹  Xianyu Piao¹  Nan Hou¹ 

[1] MOH Key Laboratory of Systems Biology of Pathogens, Institute of Pathogen Biology, Chinese Academy of Medical Sciences & Peking Union Medical College, Dong Dan San Tiao 9, Beijing, People’s Republic of China;Key Laboratory of Zoonosis, Ministry of Education, Institute of Zoonosis, Jilin University, Xi An Da Lu 5333, Changchun, People’s Republic of China

关键词: Host–parasite interaction;    DNase II homologue;    Nuclease;    Schistosoma japonicum;   

Others  :  1137000
DOI  :  10.1186/s12864-015-1319-5

 received in 2014-03-31, accepted in 2015-02-04,  发布年份 2015

【 摘 要 】

Background

Recent advances in studies of the Schistosoma japonicum genome have opened new avenues for the elucidation of parasite biology and the identification of novel targets for vaccines, drug development and early diagnostic tools.

Results

In this study, we surveyed the S. japonicum genome database for genes encoding nucleases. A total of 130 nucleases of 3 classes were found. Transcriptional analysis of these genes using a genomic DNA microarray revealed that the majority of the nucleases were differentially expressed in parasites of different developmental stages or different genders, whereas no obvious transcriptional variation was detected in parasites from different hosts. Further analysis of the putative DNases of S. japonicum revealed a novel DNase II homologue (Sjda) that contained a highly conserved catalytic domain. A recombinant Sjda-GST protein efficiently hydrolysed genomic DNA in the absence of divalent iron. Western-blot and immunofluorescence assays showed that Sjda was mainly expressed on the teguments of female adult parasites and induced early humoral immune responses in infected mice.

Conclusions

A novel DNase II homologue, Sjda, was identified in S. japonicum. Sjda was mainly distributed on the teguments of adult female parasites and possessed a typical divalent iron-independent DNA catalytic activity. This protein may play an important role in the host–parasite interaction.

【 授权许可】

   
2015 Hou et al.; licensee BioMed Central.

【 图 表 】

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