Nanostructured impedimetric lectin-based biosensor for arboviruses detection

Arboviruses have been emerging as a significant global health problem due to the recurrent epidemics. Arboviruses require the development of new diagnostic devices due to the nonspecific clinical manifestations. Herein, we report a biosensor based on cysteine (Cys), zinc oxide nanoparticles (ZnONp),...

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Published in:Talanta (Oxford) Vol. 208; p. 120338
Main Authors: Simão, Estefani P., Silva, Dammyres B.S., Cordeiro, Marli T., Gil, Laura H.V., Andrade, Cesar A.S., Oliveira, Maria D.L.
Format: Journal Article
Language:English
Published: Elsevier B.V 01-02-2020
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Summary:Arboviruses have been emerging as a significant global health problem due to the recurrent epidemics. Arboviruses require the development of new diagnostic devices due to the nonspecific clinical manifestations. Herein, we report a biosensor based on cysteine (Cys), zinc oxide nanoparticles (ZnONp), and Concanavalin A (ConA) lectin to differentiate between arboviruses infections. ConA is capable of interacting with the saccharide components of the viral capsid. In this study, we evaluated the reproducibility, sensitivity, and specificity of the sensor for the virus of Dengue type 2 (DENV2), Zika (ZIKV), Chikungunya (CHIKV), and Yellow fever (YFV). Atomic force microscopy measurements confirmed the electrode surface modification and revealed a heterogeneous topography during the biorecognition process. Cyclic voltammetry (CV) and impedance spectroscopy (EIS) were used to characterize the biosensor. The blockage of the oxidation-reduction process is related to the formation of Cys-ZnONp-ConA system on the electroactive area and its subsequent interaction with viral glycoproteins. The sensor exhibited a linear response to different concentrations of the studied arboviruses. Our study demonstrates that ConA lectin recognizes the structural glycoproteins of the DENV2, ZIKV, CHIKV, and YFV. DENV2 is the most structurally similar to ZIKV. Our results have shown that the impedimetric response correlates with the structural glycoproteins, as follow: DENV2 (18.6 kΩ) > ZIKV (14.6 kΩ) > CHIKV (6.86 kΩ) > YFV (5.98 kΩ). The homologous structural regions contribute to ConA-arboviruses recognition. Our results demonstrate the use of the proposed system for the development of biosensors for arboviruses infections. [Display omitted] •A new strategy to construct an electrochemical biosensor for arboviruses was obtained.•Our study demonstrates that ConA lectin recognizes the structural glycoproteins of the arboviruses.•We obtained a sensor platform with high sensitivity, selectivity, and a simple assembly process.
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ISSN:0039-9140
1873-3573
DOI:10.1016/j.talanta.2019.120338