| Registro completo |
| Provedor de dados: |
OAK
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| País: |
Japan
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| Título: |
Expression of truncated Babesia gibsoni thrombospondin-related adhesive proteins in Escherichia coli and evaluation of their diagnostic potential by enzyme-linked immunosorbent assay
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| Autores: |
Sandagdorj, Narantsatsral
Goo, Youn-Kyoung
Terkawi, Mohamad Alaa
Soma, Takehisa
Luo, Yuzi
Li, Yan
Cao, Shinuo
Aboge, Gabriel Oluga
Nishikawa, Yoshifumi
Badgar, Battsetseg
Xuan, Xuenan
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| Data: |
2011-10
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| Ano: |
2011
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| Palavras-chave: |
Babesia gibsoni
Diagnosis
Enzyme-linked immunosorbent assay (ELISA)
Thrombospondin-related adhesive protein (TRAP)
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| Resumo: |
Among the previously established enzyme-linked immunosorbent assays (ELISAs), an ELISA using the full length of recombinant thrombospondin-related adhesive protein of Babesia gibsoni (rBgTRAPf) is considered as the most sensitive diagnostic method for the detection of antibody to B. gibsoni in dogs. However, the expression of rBgTRAPf in high concentration is poor and thus limits its usefulness as diagnostic antigen. To improve its expression level, we have truncated BgTRAPf into two fragments having either N- or C-terminus (BgTRAPn or BgTRAPc). The expression of BgTRAPc protein in Escherichia coli yielded adequate recombinant protein. The specificity and sensitivity of ELISAs with the truncated proteins were determined using B. gibsoni-experimentally infected dog sera and specific pathogen-free (SPF) dog sera. A total of 254 field dog sera were examined by the ELISA with rBgTRAPn, rBgTRAPc and rBgTRAPf as well as by indirect fluorescent antibody test (IFAT). The specificity of rBgTRAPc was highest (97.15%) and its kappa value was more (0.8003) than rBgTRAPn (0.7083). With sufficient level of expression as well as higher specificity and reliable sensitivity, rBgTRAPc appears to be a potential candidate antigen for serodiagnosis of B. gibsoni infection in dogs.
http://www.sciencedirect.com/science/article/pii/S0014489411002165
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| Idioma: |
Inglês
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| Identificador: |
http://ir.obihiro.ac.jp/dspace/handle/10322/3115
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| Editor: |
Elsevier
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| Formato: |
application/pdf
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| Direitos: |
Elsevier
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