ArticleParasitology research2013
Immunoproteomics approach for EPC1 antigenic epitope prediction of G1 and G6 strains of Echinococcus granulosus.
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 5 papers.
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Who cites it
5 citing papers in PubMed, 12 citations in OpenAlex.
- Proteome evaluation of human cystic echinococcosis sera using two dimensional gel electrophoresis.Gastroenterology and hepatology from bed to bench · 2018Article
- A Study of Cross-Reactivity Between Recombinant EPC1 Antigen of Echinococcus granulosus in Serum from Patients with Confirmed Cystic Echinococcosis Infection and Other Parasitic Infections.The American journal of tropical medicine and hygiene · 2016Article
- Animal board invited review: advances in proteomics for animal and food sciences.Animal : an international journal of animal bioscience · 2015Review
- Cystic echinococcoses in Mongolia: molecular identification, serology and risk factors.PLoS neglected tropical diseases · 2014Article
- Evaluation of Dot Immunogold Filtration Assay (DIGFA) By Recombinant Protein EPC1 for Anti- Echinococcus granulosus IgG Antibody.Iranian journal of parasitologyArticle
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It is important to establish the diagnosis of cystic echinococcosis (CE) infection and begin control management. Currently, it is difficult to make an accurate diagnosis of CE without the availability of an accurate test, which requires the use of sensitive and specific antigens. Using recombinant antigens the sensitivity and specificity of the CE serology assays could be improved considerably. Recently, a highly antigenic protein named EPC1was characterized and isolated from an Echinococcus granulosus protoscoleces. The current study was designed to assess the sequences of EPC1 isolated from different intermediate hosts of E. granulosus. In addition, identification of a highly antigenic linear B cell epitope was found within EPC1 antigen candidate. The EPC1 sequence contains coding and non-coding regions and was compared between two predominant strains (G1 and G6) in Iran. Sequence polymorphism was not found in protein coding regions, suggesting that these regions may be useful for identification of protein expression as an antigen. The average antigenic activity for the whole protein is above 1.1, and hydrophobicity below 0 indicates that it is hydrophilic. Structural analysis showed alpha helical regions in amino acids 6-25, 35-44, 52-62, and 72-78. Nine B cell epitope residues were identified out of 67 total residues. The identity of EPC1 sequence in both G1 and G6 genotypes affects the antigenic efficacy of EPC1and suggests the recombinant protein will be useful in serological assays in the regions where the two strains are prevalent.
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