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Studying SARS-CoV-2 interactions using phage-displayed receptor binding domain as a model protein
Beatriz Pérez-Massón1, Yazmina Quintana-Pérez1, Yaima Tundidor1
1Center of Molecular Immunology, Calle 216 esq 15, apartado 16040, Atabey, Playa, CP 11300, Havana, Cuba.
Scientific Reports
|January 6, 2024
Summary
A new phage display platform allows researchers to study SARS-CoV-2 variants. This tool helps understand how mutations in the receptor binding domain (RBD) affect ACE2 interaction and antibody effectiveness, aiding in anticipating viral evolution.
Area of Science:
- Virology
- Immunology
- Biotechnology
Background:
- The SARS-CoV-2 receptor binding domain (RBD) is crucial for viral entry via ACE2 interaction.
- Neutralizing antibodies primarily target the RBD, making it a key focus for vaccine and therapeutic development.
- RBD sequence variability necessitates methods to study evolving variants and their interactions.
Purpose of the Study:
- To develop a simple phage display platform for analyzing SARS-CoV-2 RBD variants.
- To investigate the complex interactions between mutated RBDs, ACE2, and neutralizing antibodies.
- To identify critical residues and mutations affecting RBD-ACE2 binding and antibody inhibition.
Main Methods:
- Display of wild-type and mutated Wuhan-Hu-1 RBD on filamentous phages.
- Phage-based mutational scanning to assess RBD plasticity and critical residues.
- Evaluation of vaccine-induced antibody inhibition of RBD variants binding to ACE2.
Main Results:
- Successful display of biologically active and antigenic RBD variants on phage.
- Identification of key residues and mutations influencing RBD-ACE2 interactions, including those that strengthen binding.
- Demonstration that vaccine-induced antibodies can inhibit ACE2 binding of many RBD variants, though effectiveness varies.
- Pinpointing specific amino acid changes that may reduce antibody efficacy.
Conclusions:
- The developed phage display platform is effective for studying SARS-CoV-2 RBD diversity.
- This approach aids in understanding structure-function relationships and anticipating viral evolution.
- The platform can be expanded for large-scale analysis of SARS-CoV-2 and related coronaviruses, supporting protein engineering and pandemic preparedness.
