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Published on: March 15, 2019
Antibody numbering schemes: advances, comparisons and tools for antibody engineering
Zirui Zhu1,2, Hossein Ashrafian1,2, Navid Mohammadian Tabrizi1,2
1Department of Chemistry and Biochemistry, The Ohio State University, 151 W. Woodruff Ave. Columbus, OH 43210, United States of America.
None:
The evolution of antibody engineering has significantly enhanced the development of antibody-based therapeutics, enabling the creation of novel antibody formats tailored for specific applications. Since the introduction of the Kabat numbering scheme in 1977, various schemes have been developed and modified, forming the foundation for multiple antibody engineering projects. The tools associated with these schemes further facilitate the engineering process. However, discrepancies among current numbering schemes can lead to confusion. This study examines various numbering schemes and related tools, providing new insights into antibody variable domains. Improved understanding of antibody numbering and related tools holds significant potential for more precise and efficient antibody design, thereby advancing antibody-based therapeutics and diagnostics.
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Antibody Structure
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
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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.

