ArticleParasitology research2013
Cloning and characterization of the fatty acid-binding protein gene from the protoscolex of Taenia multiceps.
Article in Parasitology research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Evaluation of recombinant Taenia multiceps HSP70 antigen in a dipstick-based rapid diagnostic test for ovine coenurosis.BMC veterinary research · 2026Article
- Comparative Transcriptome Analyses of the Developmental Stages ofFrontiers in veterinary science · 2021Article
- Molecular characterisation and expression analysis of two heat-shock proteins in Taenia multiceps.Parasites & vectors · 2019Article
- Article
- De novo genome and transcriptome analyses provide insights into the biology of the trematode human parasite Fasciolopsis buski.PloS one · 2018Article
- Molecular cloing and bioinformatics analysis of lactate dehydrogenase from Taenia multiceps.Parasitology research · 2017Article
- Characterization of a Secretory Annexin in Echinococcus granulosus.The American journal of tropical medicine and hygiene · 2016Article
- Expression and immunolocalisation of TpFABP as a candidate antigen for the serodiagnosis of rabbit Taenia pisiformis cysticercosis.Parasite (Paris, France) · 2013Article
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Taenia multiceps (Cestoda: Taeniidae), a worldwide cestode parasite, is emerging as an important helminthic zoonosis due to serious or fatal central nervous system disease commonly known as coenurosis in domestic and wild ruminants including humans. Herein, a fatty acid-binding protein (FABP) gene was identified from transcriptomic data in T. multiceps. This gene, which contains a complete coding sequence, was amplified by reverse-transcriptase polymerase chain reaction. The corresponding protein, which was named TmFABP, had a molecular weight of 14 kDa, and subsequently was recombinantly expressed in Escherichia coli. The fusion protein was purified on Ni-NTA beads (Bio-Rad). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blot analyses showed that the purified recombinant protein caused immunogenicity. Immunohistochemical studies showed that TmFABP was expressed at the tegumental level in the protoscolices and in the cells between the body wall and parenchyma layer of the cestode. In sections from gravid proglottids, intense staining was detected in the uterus and eggs. Based on this, TmFABP could be switched on during differentiation of germinative layers to protoscoleces and from metacestodes to adult worms. Taken together, our results already reported for T. multiceps suggest the possibility of TmFABP developing a vaccine to control and prevent coenurosis.
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