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Evolution of immunoglobulin M (IgM) structure and function in vertebrates: A comprehensive review
Shun Yang1, Lu-Chuan Zhao2, Fu-Zhen Guo2
1College of Life Sciences and Medicine, Zhejiang Sci-Tech University, Hangzhou, 310018, China; Zhejiang Provincial Engineering Research Center of New Technologies and Applications for Targeted Therapy of Major Diseases, Zhejiang Sci-Tech University, Hangzhou, 310018, China.
Fish & Shellfish Immunology
|August 6, 2025
Summary
Immunoglobulin M (IgM), a key antibody, evolved complex structures and functions across vertebrates. Its evolutionary journey reveals how IgM multimerization co-evolved with specialized immunity.
Area of Science:
- Immunology
- Evolutionary Biology
- Structural Biology
Background:
- Immunoglobulin M (IgM) is a crucial antibody isotype in vertebrate immunity.
- It is the earliest antibody class to emerge in jawed vertebrates.
- IgM's structure and function have adapted over 500 million years.
Purpose of the Study:
- To systematically review the evolutionary history of IgM.
- To explore the link between IgM's structural variations and functional specialization.
- To propose a hypothesis on the co-evolution of IgM multimerization and function.
Main Methods:
- Literature review and synthesis of existing knowledge.
- Integrated analysis of structural and functional data.
- Comparative evolutionary trajectory examination from cartilaginous fish to mammals.
Main Results:
- IgM exhibits significant structural and functional adaptations throughout vertebrate evolution.
- Multimeric structural variations in IgM are intrinsically linked to its specialized functions.
- A novel hypothesis is proposed regarding the co-evolution of IgM multimerization patterns and functional specialization.
Conclusions:
- Understanding IgM evolution offers insights into the origins of adaptive immunity.
- IgM's evolutionary path highlights the interplay between structure, multimerization, and function.
- Further research into IgM evolution can inform novel therapeutic strategies.
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