Cell & Developmental Biology
Open Access

Characteristics of Antibodies and B-Cells

Gaandla Nikhitha^{* *}Correspondence: Gaandla Nikhitha, Department of Pharmacology, Malla Reddy College of Pharmacy, Jawaharlal Nehru Technological University Hyderabad, Hyderabad, India, Email:

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Description

Antibodies protect vertebrates from infection by neutralizing viruses and microbial toxins and engaging the complement system and different types of white blood cells to eradicate the aggressive pathogens. A typical antibody molecule is Y-shaped, having binding sites for complement proteins and other cellsurface receptors on the tail of the Y. The two tips of the Y have two identical antigen-binding sites. A distinct antigen-binding site is present in each antibody molecule produced by a B cell clone. The antibody molecules are initially inserted into the plasma membrane during B cell formation in the bone marrow, where they serve as antigen receptors. When antigen attaches to these receptors in peripheral lymphoid organs, helper T cells' stimulatory signals activate the B cells, causing them to multiply and develop into memory cells or effector cells that secrete antibodies. The same unique antigen-binding location that the membrane-bound antibodies have is also secreted by the effector cells' antibodies. Four polypeptide chains, two identical heavy chains and two identical light chains make up the average antibody molecule. The antigen-binding sites are often formed by the combination of portions of both the heavy and light chains. IgA, IgD, IgE, IgG, and IgM are the five classes of antibodies. Each has a unique heavy chain (α, δ, ε, γ, and μ, respectively). The heavy chains also make up the antibody's tail (Fc region), which controls other proteins attach to it and consequently, biological characteristics of the antibody class contains. Any class of heavy chain can be coupled with any type of light chain (or both), but other than antigen specificity, the light chain type does not appear to affect the characteristics of the antibody. Ig domains, sheet structures with roughly 110 amino acids each, make up the majority of each light and heavy chain. While a heavy chain has one variable (VH) and three or four constant (CH) domains, a light chain only have one variable (VL) and one constant (CL) domain. The light and heavy chains' variable domain amino acid sequence variation is mostly restricted to a few discrete hyper variable areas that protrude as loops at one end of the domains to create the antigen-binding site.

B Cells and antibodies

If they are unable to produce antibodies, vertebrates will surely die to infection. By attaching to viruses and microbial toxins, antibodies protect us against infection by neutralizing them. A system of blood proteins known as complement and several types of white blood cells are also enlisted by antibodies that bind to invading invaders. To attack the invaders, the white blood cells and complement-activated components cooperate.

Conclusion

Antibodies are only made by B cells, and there are billions of different types of them, each with a unique amino acid sequence and antigen-binding site. Immunoglobulins, also referred to collectively as Ig, are among the most prevalent proteins found in blood, making up around 20% of the total protein in plasma by weight. Five different kinds of antibodies are produced by mammals, and each class causes a distinct biological reaction in response to antigen binding. The composition, purpose, and interactions between antibodies and antigen are covered in this section.