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    Investigation of SARS-CoV-2 nucleocapsid protein interaction with a specific antibody by combined spectroscopic ellipsometry and quartz crystal microbalance with dissipation

    Journal: J. Colloid Interface Sci., Volume 626, NOV 15, page 113–122

    Authors: Plikusiene, Ieva; Maciulis, Vincentas; Juciute, Silvija; Ramanavicius, Arunas; Balevicius, Zigmas; Slibinskas, Rimantas; Kucinskaite-Kodze, Indre; Simanavicius, Martynas; Balevicius, Saulius; Ramanaviciene, Almira

    Organizations: European Regional Development Fund [13.1.1-LMT-K-718-05-0033]; Research Council of Lithuania (LMTLT); Lithuanian National Commission for UNESCO; Lithuanian Academy of Sciences

    Keywords: SARS-CoV-2; Quartz crystal microbalance with; dissipation (QCM-D); Spectroscopic ellipsometry; Antibody and antigen interaction; Immunosensor; Antibody flexibility; Antibody bivalent binding

    Detailed evaluations of the antigen and antibody interaction rate and strength of the immune complex formed are very important for medical and bioanalytical applications. These data are crucial for the development of sensitive and fast immunosensors suitable for continuous measurements. Therefore, combined spectroscopic ellipsometry (SE) and quartz crystal microbalance with dissipation (QCM-D) technique (SE/ QCM-D) was used for the evaluation: (i) of covalent immobilization of SARS-CoV-2 nucleocapsid protein (SCoV2-N) on QCM-D sensor disc modified by self-assembled monolayer based on 11mercaptoundecanoic acid and (ii) interaction of immobilized SCoV2-N with specific polyclonal antiSCoV2-N antibodies followed by immune complex formation process. The results show that the SCoV2-N monolayer is rigid due to the low energy dissipation registered during the QCM-D measurement. In contrast, the anti-SCoV2-N layer produced after interaction with the immobilized SCoV2-N formed a soft and viscous layer. It was determined, that the sparse distribution of SCoV2-N on the surface affected the spatial arrangement of the antibody during the formation of immune complexes. The hinge-mediated flexibility of the antibody Fab fragments allows them to reach the more distantly located SCoV2-N and establish a bivalent binding between proteins in the formed SCoV2-N/anti-SCoV2-N complex. It was noted that the SE/QCM-D method can provide more precise quantitative information about the flexibility and conformational changes of antibody during the formation of the immune complex on the surface over time.(c) 2022 Published by Elsevier Inc.
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