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Toxicon ; 92: 186-92, 2014 Dec 15.
Artigo em Inglês | MEDLINE | ID: mdl-25448390

RESUMO

The variable domain of the heavy-chain-only antibody (VHH) or nanobody (Nb), derived from camelids, begins to play an important role on the detection of protein markers. In this study, we constructed a phage-displayed library of VHHs against Cry1Fa by immunizing a healthy Bactrian camel with Cry1Fa toxin. After a series of bio-panning and screening by phage display technology, three anti-Cry1Fa nanobodies (Nbs) with great difference in complementarity determining region 3 (CDR3) were obtained and they were highly specific to Cry1Fa as well as showed full of activity when exposed to 70 °C for 3 h. Through modifying Nbs with Horseradish Peroxidase (HRP) and biotin, two Nbs which can recognize the different epitopes of Cry1Fa were determined and they were used to establish a novel sandwich immune ELISA based on biotin-SA interaction for Cry1Fa detection. The immunoassay exhibited a linear range from 1 to 100 ng/mL with a detection limit of 0.88 ng/mL. The recoveries from spiked corn and soybean samples were ranged from 83.33 to 117.17%, with a coefficient of variation (C.V) less than 6.0%. All together, the proposed immunoassay will be a promising way for sensitive and accurate determination of Cry1Fa toxin.


Assuntos
Proteínas de Bactérias/imunologia , Camelus/imunologia , Endotoxinas/imunologia , Proteínas Hemolisinas/imunologia , Imunoensaio/métodos , Anticorpos de Domínio Único/isolamento & purificação , Animais , Toxinas de Bacillus thuringiensis , Ensaio de Imunoadsorção Enzimática , Mapeamento de Epitopos , Escherichia coli , Adjuvante de Freund , Biblioteca de Peptídeos
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