ArticleParasitology research2008
Molecular characterization of a calcium-binding protein SjCa8 from Schistosoma japonicum.
Article in Parasitology research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Calmodulin disruption impacts growth and motility in juvenile liver fluke.Parasites & vectors · 2016Article
- Schistosoma japonicum tegumental protein 20.8, role in reproduction through its calcium binding ability.Parasitology research · 2014Article
- An EF-handed Ca(2+)-binding protein of Chinese liver fluke Clonorchis sinensis.Parasitology research · 2013Article
- Molecular identification, immunolocalization, and characterization of Clonorchis sinensis calmodulin.Parasitology research · 2013Article
- FhCaBP4: a Fasciola hepatica calcium-binding protein with EF-hand and dynein light chain domains.Parasitology research · 2012Article
- Cloning, expression, and characterization of a novel Opisthorchis viverrini calcium-binding EF-hand protein.Parasitology international · 2012Article
- Cloning and functional characterization of two calmodulin genes during larval development in the parasitic flatworm Schistosoma mansoni.The Journal of parasitology · 2011Article
- Cloning, molecular characterization of a 13-kDa antigen from Schistosoma japonicum, Sj13, a putative salivary diagnosis candidate for Schistosomiasis japonica.Parasitology research · 2009Article
- Expression profile, localization of an 8-kDa calcium-binding protein from Schistosoma japonicum (SjCa8), and vaccine potential of recombinant SjCa8 (rSjCa8) against infections in mice.Parasitology research · 2009Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A full-length cDNA encoding a cercarial stage-specifically expressed 8-kDa calcium-binding protein (SjCa8) was isolated from Schistosoma japonicum cercarial cDNA library using microarray screen. The putative gene coding for SjCa8 is of 371 bp with an open reading frame of 69 amino acid (aa). The deduced aa sequence showed 83% identity with the Schistosoma mansoni 8-kDa CaBP, 47% identity with Clonorchis sinensis calcium-binding protein, and 38% identity with Fasciola hepatica putative calcium-binding protein. Also, it shares more than 30% identity with the calmodulin of many different species, while the most significant similarity between them lies around the two calcium-binding loop regions. There are two potential sites for phosphorylation and one potential site for N-myristoylation in the sequence. The SjCa8 has also been predicted to contain a single pair of EF-hand Ca2+-binding domain. The recombinant SjCa8 (rSjCa8) protein expressed and purified from E. coli has been demonstrated to possess the calcium-binding activity. Immune serum from UV-attenuated S. japonicum cercariae-immunized rabbit detected rSjCa8 by Western blot assay, while the sera from S. japonicum naturally infected rabbit and normal rabbit could not. These findings may contribute to the development of an effective vaccine against schistosomiasis.
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