免疫球蛋白同型进化的Janus (双) 模型:保存和可塑性是定义范式的
1Department of Microbiology and Immunology, University of Maryland School of Medicine, Baltimore, Maryland, USA.
Immunological reviews
|September 3, 2024
概括
脊椎动物中的抗体进化揭示了令人着迷的保护和灵活性历史. 研究从软骨鱼到两动物的免疫球蛋白 (Igs) 展示了自适应性免疫系统的发展和各种抗体功能.
科学领域:
- 免疫学 免疫学 免疫学
- 进化生物学 进化生物学
- 脊椎动物动物学的比较.
背景情况:
- 人类免疫球蛋白 (Igs) 从脊椎动物 (gnathostomes) 中存在的祖先形式进化.
- 抗体进化表明了保留特征和适应性灵活性之间的平衡.
- 关键的进化里程碑包括Ig重链 (H) 同型的出现,如IgM和IgD/W.
研究的目的:
- 提供跨脊椎动物类抗体演变的概述.
- 突出免疫球蛋白的关键适应策略和功能多样化.
- 为了用令人着迷的抗体适应的进化编年史来吸引读者.
主要方法:
- 在脊椎动物血统中对免疫球蛋白结构和功能的比较分析.
- 关于软骨鱼,两动物和其他脊椎动物抗体进化的现有文献的综述.
- 强调抗体适应不同生态的具体例子.
主要成果:
- 软骨鱼的Igs代表了抗体进化的早期阶段.
- 两动物显示出Ig同型切换和IgG类分子的出现.
- 不同的适应机制包括单域变量区域,适应寒冷的Igs和粘膜防御策略.
结论:
- 抗体进化是一个动态的过程,其特点是可性,融合和保存.
- 对脊椎动物抗体的研究为适应性免疫系统的起源和多样化提供了深刻的见解.
- 对粘膜Ig进化和其他适应策略的进一步研究是有必要的.
更多相关视频
06:15Characterization of Thymus-dependent and Thymus-independent Immunoglobulin Isotype Responses in Mice Using Enzyme-linked Immunosorbent Assay
Published on: September 7, 2018
9.4K
09:49Induction and Assessment of Class Switch Recombination in Purified Murine B Cells
Published on: August 13, 2010
19.0K
相关概念视频
Antibody Structure
59.6K
Overview
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...
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...
59.6K
Diversity of Antigen Receptors
543
Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...
543
Antibody Structure and Classes
856
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.
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.
856
Conservation of Protein Domains Over Different Proteins
10.8K
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
10.8K
Immunoglobulin-like Cell Adhesion Molecules
3.2K
Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
3.2K
Cells of the Adaptive Immune Response
972
The T and B lymphocytes of the adaptive immune system develop from common lymphoid progenitor cells in the bone marrow. These progenitors give rise to precursors that eventually develop into both T and B lymphocytes. As these precursors mature, they gain the ability to detect and respond to foreign antigens in the body, a process known as immunocompetence. Additionally, these precursors acquire self-tolerance, a process that ensures they do not react to self-antigens. This intricate system...
972
