サポート>ブログ>抗体アイソタイプ:IgG

抗体アイソタイプ:IgG

Biointron 2024-01-20
IgG.jpg
Image credit: DOI: 10.1016/B978-0-12-374279-7.05002-5

Immunoglobulins, also known as antibodies, are heterodimeric proteins made up of two heavy (H) chains and two light (L) chains. They can be classified into five primary isotypes (IgG, IgA, IgD, IgE, and IgM) determined by the constant domains in their H chains, which give each isotype their different characteristics.

Immunoglobulin G is the most abundant subtype, being present in the largest concentrations at 75-80% of IgGs in blood and tissue fluids. IgG makes direct impacts on the immune response with high neutralization and opsonization activities towards toxins and viruses, acting as the first line of defense after memory B cells trigger a response. They are responsible for both existing and acquired immunity against previously encountered antigens. Once IgG binds to antigens, the Fc receptor can bind to macrophages, which can carry out phagocytosis on the intruder.1,2

Uniquely, IgG can also cross the placenta and impart immunity to the fetus. This occurs through transcytosis, in which the IgG is endocytosed and shuttled across the cytoplasm to be secreted towards the basal cell membrane of syncytiotrophoblasts. Once there, the complex is released into fetal circulation.

IgG can be further classified into: IgG1, IgG2, IgG3, and IgG4. All four subtypes exhibit different functional activities. For example, with a HIV patient, IgG3 antibodies have been demonstrated to be more effective at neutralizing HIV over IgG1, likely because of differing antibody flexibility affecting access and how changes are induced in the virus’ oligomer structure.3

At Biointron, we are dedicated to accelerating your antibody discovery, optimization, and production needs. Our team of experts can provide customized solutions that meet your specific research needs. Contact us to learn more about our services and how we can help accelerate your research and drug development projects.


References:

  1. Schroeder, H. W., & Cavacini, L. (2010). Structure and Function of Immunoglobulins. The Journal of Allergy and Clinical Immunology, 125(2 0 2), S41. https://doi.org/10.1016/J.JACI.2009.09.046 

  2. Borad, S. G., & Singh, A. K. (2022). Immunoglobulins. Encyclopedia of Dairy Sciences, 894–900. https://doi.org/10.1016/B978-0-12-818766-1.00367-6 

  3. Ciobanu, A. M., Dumitru, A. E., Gica, N., Botezatu, R., Peltecu, G., & Panaitescu, A. M. (2020). Benefits and Risks of IgG Transplacental Transfer. Diagnostics, 10(8). https://doi.org/10.3390/DIAGNOSTICS10080583 


Subscribe to our ブログ
Recommended Articles
人間の免疫システムの活用:自然な防御から精密医療へ

免疫・PAMP/DAMP・革新的抗体療法の解説

Aug 08, 2025
抗体薬物複合体(ADC)の基礎レビュー:作用機序、臨床進展、設計最適化、課題、および将来

抗体薬物複合体(Antibody-Drug Conjugates, ADC)は、がん治療において革新的なターゲット型治療薬の一つであり、モノクローナル抗体(mA……

Aug 05, 2025
抗体機能におけるFc糖鎖の役割

抗体の機能は、Fc領域の糖鎖修飾状態に大きく依存しています。

Jun 25, 2025
AIS 2025 – フランス:ハイライトとイベント総括

第13回抗体産業シンポジウム(Antibody Industrial Symposium 2025)が、2025年6月25日から26日にかけてフランス・トゥール……

Jun 22, 2025

お客様の利便性を向上させるためにクッキーを使用しています。詳しくは プライバシーポリシー をご覧ください。