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Production of monoclonal antibodies explained

Infection and responseMonoclonal antibodies (biology only) (HT only)

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What happens if the antigen epitope mutates?

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The monoclonal antibody may no longer bind because the complementary binding site no longer matches.

Key concepts

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Definition of monoclonal antibodies

Monoclonal antibodies are identical antibodies produced by many copies of a single cell. The term 'mono' indicates one type and 'clonal' indicates that every antibody molecule comes from the same original antibody‑producing cell. Production of identical antibodies requires cloning of a single hybridoma cell that produces the antibody with a single, unique binding site.

Stimulating lymphocytes to make the antibody

An antigen of interest is injected into a mouse to stimulate its immune system. Lymphocytes in the spleen respond by producing antibodies specific to the injected antigen. Spleen cells are collected because they contain the antibody‑producing B lymphocytes. The immune stimulation step generates cells that produce antibodies matching the antigen’s binding site.

Fusion with myeloma (tumour) cells to form hybridomas

Antibody‑producing spleen cells are fused with myeloma cells (cancerous white blood cells) to form hybridoma cells. Myeloma cells provide the ability to grow indefinitely in culture, while the spleen cells provide the antibody specificity. Fusion produces hybridoma cells that both divide continuously and secrete the desired antibody. Unfused myeloma cells cannot survive in the selective growth medium and die, leaving hybridomas to be cultured.

Cloning and selection of a single hybridoma

A single hybridoma cell that produces the required antibody is isolated and cloned by cell division. Cloning produces a large population of genetically identical hybridoma cells - a single clone - that all secrete the same antibody. Antibodies collected from this culture are therefore identical and specific to one binding site on the antigen. Purification from the culture medium uses methods such as centrifugation, filtration and chromatography.

Molecular basis of specificity

Each antibody molecule has a variable region that forms a binding site complementary to a specific antigen epitope (part of a protein antigen). A single B lymphocyte produces antibodies with one unique variable region; cloning that B cell (via the hybridoma route) preserves that single binding site across all antibody molecules produced. The lock‑and‑key fit between antibody binding site and antigen epitope explains high specificity.

Key notes

Important points to keep in mind

Antigen injection into a mouse stimulates spleen B lymphocytes that produce antibodies specific to that antigen.

Fusion of spleen cells with myeloma cells produces hybridomas that both secrete antibody and divide indefinitely.

Selective culture medium removes unfused myeloma cells; surviving hybridomas are cloned to make monoclonal populations.

Monoclonal antibodies come from one clone and therefore recognise one epitope on one protein antigen.

Antibody–antigen binding depends on complementary shape between an antibody variable region and an antigen epitope (lock‑and‑key).

Cloning ensures batch uniformity; antigen changes or masked epitopes prevent binding and limit effectiveness.

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