Phosphoglycan-sensitized platform for specific detection of anti-glycan IgG and IgM antibodies in serum.

Talanta

Max Planck Tandem Group in Nanobioengineering, University of Antioquia, Complejo Ruta N, Calle 67 N° 52-20, Medellín, 050010, Colombia. Electronic address:

Published: September 2020

Glycosylphosphatidylinositol anchored proteins (GPI-APs) are natural conjugates in the plasma membrane of eukaryotic cells that result from the attachment of a glycolipid to the C-terminus of many proteins. GPI-APs play a crucial role in cell signaling and adhesion and have implications in health and diseases. GPI-APs and GPIs without protein (free GPIs) are found in abundance on the surface of the protozoan parasite Toxoplasma gondii. The detection of anti-GPI IgG and IgM antibodies allows differentiation between toxoplasmosis patients and healthy individuals using serological assays. However, these methods are limited by their poor efficiency, cross-reactivity and need for sophisticated laboratory equipment and qualified personnel. Here, we established a label-free electrochemical glycobiosensor for the detection of anti-GPI IgG and IgM antibodies in serum from toxoplasmosis seropositive patients. This biosensor uses a synthetic GPI phosphoglycan bioreceptor immobilized on screen-printed gold electrodes through a linear alkane thiol phosphodiester. The antigen-antibody interaction was detected and quantified by electrochemical impedance spectroscopy (EIS). The resultant device showed a linear dynamic range of anti-GPI antibodies in serum ranging from 1.0 to 10.0 IU mL, with a limit of detection of 0.31 IU mL. This method also holds great potential for the detection of IgG antibodies related to other multiple medical conditions characterized by overexpression of antibodies.

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http://dx.doi.org/10.1016/j.talanta.2020.121117DOI Listing

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