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Related Concept Videos

Antibody Structure and Classes01:25

Antibody Structure and Classes

8.1K
Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
8.1K

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Use of an Influenza Antigen Microarray to Measure the Breadth of Serum Antibodies Across Virus Subtypes
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MAAD: multidimensional antiviral antibody database.

Yixin Li1,2, Jinyue Wang1,2, Chuziyue Zhang1,2,3

  • 1State Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.

Protein & Cell
|December 6, 2025
PubMed
Summary

The Multidimensional Antiviral Antibody Database (MAAD) offers a standardized platform for exploring antibody sequence, structure, and function. This resource aids in comparative antiviral research and the rational design of therapeutic antibodies.

Keywords:
RNA virusesantibody databaserational antibody designsequence–structure–function integration

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Area of Science:

  • Immunology and Virology
  • Bioinformatics and Computational Biology
  • Drug Discovery and Development

Background:

  • Antibodies are crucial for preventing and treating viral infections.
  • Current antibody discovery is shifting from screening to rational design, requiring integrated sequence-structure-function data.
  • Existing resources lack standardization and comprehensive multidimensional features for antiviral antibodies.

Purpose of the Study:

  • To introduce the Multidimensional Antiviral Antibody Database (MAAD) as a standardized, curated resource.
  • To integrate multidimensional features of antibodies targeting high-impact RNA viruses.
  • To facilitate systematic exploration, cross-pathogen comparison, and rational antibody design.

Main Methods:

  • Developed MAAD, a database focusing on Coronaviridae, Orthomyxoviridae, and Pneumoviridae.
  • Incorporated interactive analysis modules for CDR/germline annotation, sequence analysis, clustering, and interface residue identification.
  • Included per-site entropy and mutation rate profiling for in-depth sequence characteristic exploration.

Main Results:

  • MAAD provides a comprehensive, curated dataset of antiviral antibodies, nanobodies, and single-chain variable fragments.
  • Interactive modules enable detailed analysis of antibody sequence, structure, and functional relationships.
  • The platform supports structure-guided identification of critical antibody residues and mutation profiles.

Conclusions:

  • MAAD bridges antibody sequence, structure, and function for advanced research.
  • The database offers an open and standardized platform for comparative antiviral research.
  • MAAD significantly supports and advances the discovery and rational design of therapeutic antibodies.