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Diversity of Antigen Receptors

Diversity of Antigen Receptors

Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
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Complex Mutation Pattern of Omicron BA.2: Evading Antibodies without Losing Receptor Interactions.

Saathvik R Kannan¹, Austin N Spratt¹, Kalicharan Sharma²

¹Bond Life Sciences Center, University of Missouri, Columbia, MO 65211, USA.

International Journal of Molecular Sciences

|May 28, 2022

Summary

The Omicron BA.2 sublineage, now dominant globally, shows increased infectivity due to unique mutations. These changes enhance receptor binding and antibody evasion compared to BA.1.

Keywords:

BA.2 COVID-19 Delta Omicron BA.1 SARS-CoV-2 viruses

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Last Updated: Sep 21, 2025

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Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

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Published on: March 24, 2017

Area of Science:

Virology
Molecular Biology
Epidemiology

Background:

Omicron BA.2, a sublineage of Omicron BA.1, is globally prominent.
Early data suggests BA.2 exhibits higher infectivity than BA.1.

Purpose of the Study:

To analyze the mutation profile of BA.2.
To understand the impact of these mutations on receptor interactions and antibody binding.
To investigate the molecular basis for BA.2's increased infectivity.

Main Methods:

Analysis of available SARS-CoV-2 sequences.
Examination of Spike protein structures complexed with receptors and antibodies.
Molecular dynamics simulations.

Main Results:

BA.2 possesses 50 high-prevalent mutations, with 19 unique mutations and a Delta variant signature (G142D).
Receptor-binding domain (RBD) mutations in BA.2 (G446/G496) enhance stability compared to BA.1 (S446/S496).
Molecular dynamics simulations indicate BA.2 exhibits greater antibody evasion than BA.1.

Conclusions:

BA.2 evolved novel mutations to maintain wild-type-like receptor binding.
These mutations facilitate enhanced antibody evasion compared to BA.1.
The acquisition of Delta variant mutations may contribute to BA.2's high infectivity.