Cross-reaction mediated by distinct key amino acid combinations in the complementary-determining region (CDR) of a monoclonal antibody

Guo, Chunyan, Feng, Qing, Xie, Xin, Li, Yan, Hu, Hanyu, Hu, Jun, Fang, Senbiao and Shang, Lijun (2024) Cross-reaction mediated by distinct key amino acid combinations in the complementary-determining region (CDR) of a monoclonal antibody. Journal of Medical Virology, 96 (2) (e29430). pp. 1-12. ISSN 1096-9071

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Abstract / Description

In immunology, cross-reaction between antigens and antibodies are commonly observed. Prior research has shown that various monoclonal antibodies (mAbs) can recognize a broad spectrum of epitopes related to influenza viruses. However, existing theories on cross-reactions fall short in explaining the phenomena observed. This study explored the interaction characteristics of H1-74 mAb with three peptides: two natural peptides, LVLWGIHHP and LPFQNI, derived from the hemagglutinin (HA) antigen of the H1N1 influenza virus, and one synthetic peptide, WPFQNY. Our findings indicate that the complementarity-determining region (CDR) of H1-74 mAb comprised five antigen-binding sites, containing eight key amino acid residues from the light chain variable region and 16 from the heavy chain variable region. These critical residues formed distinct hydrophobic or hydrophilic clusters and functional groups within the binding sites, facilitating interaction with antigen epitopes through hydrogen bonding, salt bridge formation, and π–π stacking. The study revealed that the formation of the antibody molecule led to the creation of binding groups and small units in the CDR, allowing the antibody to attach to a variety of antigen epitopes through diverse combinations of these small units and functional groups. This unique ability of the antibody to bind with antigen epitopes provides a new molecular basis for explaining the phenomenon of antibody cross-reaction.

Item Type: Article
Uncontrolled Keywords: cross‐reaction; epitope; immunodominant groups; key amino acid residues; molecular; simulation
Subjects: 500 Natural Sciences and Mathematics > 570 Life sciences; biology
Department: School of Human Sciences
Depositing User: Lijun Shang
Date Deposited: 30 Jan 2024 10:41
Last Modified: 05 Feb 2024 16:02


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