The human immune system uses a variety of tools to protect the body from foreign pathogens. A key component of this defense network is immune gamma globulins—antibodies that help identify and neutralize invading microorganisms. Made by white blood cells called B lymphocytes or B cells, immune gamma globulins are Y-shaped proteins that circulate in the bloodstream and lymph fluid. They act as sentries, patrolling the body for anything they recognize as non-self. When an immune gamma globulin encounters its specific antigen (the term for the target microbe or substance), an immune response is triggered to eliminate the threat. This article explores the structure and functions of immune gamma globulins, as well as how they work together with other immune cells and molecules.

Immunoglobulin Structure

All Immunoglobulin share a basic architecture comprised of four peptide chains—two identical heavy chains and two identical light chains bonded together by disulfide bridges. The specific type of amino acid sequences in the variable regions at the ends of the immune gamma globulin confer its ability to bind to a single antigen. These regions allow for recognition and attachment capabilities. The constant regions make up the rest of the molecule and help classify immune gamma globulins into different classes based on their biological activity. The major classes in humans are: IgG, IgA, IgM, IgD, and IgE.

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