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Detection of SARS-CoV-2 Receptor-Binding Domain Antibody using a HiBiT-Based Bioreporter
Published on: August 12, 2021
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In silico antibody engineering for SARS-CoV-2 detection
Didac Martí1, Eduard Martín-Martínez1, Juan Torras1,2
1Departament d'Enginyeria Química, EEBE, Universitat Politècnica de Catalunya, C/ Eduard Maristany, 10-14, Ed. I2, 08019 Barcelona, Spain.
Computational and Structural Biotechnology Journal
|October 13, 2021
Summary
Engineered immunoglobulin-G (IgG) antibodies were designed for COVID-19 detection biosensors. The IgG1-S309 construct demonstrated superior stability and potential for accurate diagnostic applications.
Area of Science:
- Biotechnology
- Immunology
- Structural Biology
Background:
- Engineered immunoglobulin-G (IgG) molecules are crucial for developing protein-based biosensors for clinical diagnostics.
- Current design strategies involve merging native IgG structures with specific antibody fragments.
Purpose of the Study:
- To propose and evaluate two novel IgG-like antibodies for COVID-19 detection using molecular dynamics simulations.
- To assess the stability and suitability of engineered antibodies for biosensor applications.
Main Methods:
- Utilized conventional and accelerated classical molecular dynamics (cMD and aMD) simulations.
- Merged IgG1 B12 antibody structure with CR3022 and S309 antibody Fab fragments targeting SARS-CoV-2 receptor-binding domain (RBD).
- Immobilized engineered antibodies (IgG1-CR3022 and IgG1-S309) on a gold surface via a linker.
Main Results:
- Analyzed the stability of the two engineered antibodies (IgG1-CR3022 and IgG1-S309) on a gold surface.
- Determined that the IgG1-S309 antibody better preserved its neutralizing structure compared to IgG1-CR3022.
- Identified IgG1-S309 as a promising candidate for antibody-based COVID-19 diagnostic sensors.
Conclusions:
- The IgG1-S309 antibody is well-suited for developing effective antibody-based sensors for COVID-19 diagnosis.
- The study highlights the importance of the merging strategy and substrate in maintaining antibody stability and function.
