Tuesday, March 17, 2015

Abstract-Label-free detection and characterization of the binding of hemagglutinin protein and broadly neutralizing monoclonal antibodies using terahertz spectroscopy

Yiwen SunJunlan Zhong
Shenzhen University, School of Medicine, National-Regional Key Technology Engineering Laboratory for Medical Ultrasound, Guangdong Key Laboratory for Biomedical Measurements and Ultrasound Imaging, Department of Biomedical Engineering, Shenzhen 518060, China
Cunlin ZhangJian Zuo
Capital Normal University, Department of Physics, Beijing 100037, China
Emma Pickwell-MacPherson
Chinese University of Hong Kong, Department of Electronic Engineering, Shatin, Hong Kong
J. Biomed. Opt. 20(3), 037006 (Mar 10, 2015). doi:10.1117/1.JBO.20.3.037006

Abstract.  Hemagglutinin (HA) is the main surface glycoprotein of the influenza A virus. The H9N2 subtype influenza A virus is recognized as the most possible pandemic strain as it has crossed the species barrier, infecting swine and humans. We use terahertz spectroscopy to study the hydration shell formation around H9 subtype influenza A virus’s HA protein (H9 HA) as well as the detection of antigen binding of H9 HA with the broadly neutralizing monoclonal antibody. We observe a remarkable concentration dependent nonlinear response of the H9 HA, which reveals the formation process of the hydration shell around H9 HA molecules. Furthermore, we show that terahertz dielectric properties of the H9 HA are strongly affected by the presence of the monoclonal antibody F10 and that the terahertz dielectric loss tangent can be used to detect the antibody binding at lower concentrations than the standard ELISA test.
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