Antivenom

Antivenom is a preparation of antibodies or antibody fragments that bind and neutralize toxins in venom. It is produced by immunizing animals or, increasingly, through engineered antibody methods.

Antibody: An immune-system protein that binds a specific target, such as a toxin, pathogen, or cell-surface molecule. Antivenom’s active ingredients are antibodies selected to bind venom components.
Albert Calmette: A French physician and bacteriologist who developed an early antivenom for cobra bites in the 1890s. His work helped establish serum therapy against snake venom.
Snakebite: A bite from a snake that may inject venom into a person or animal. Snakebite is the most familiar setting for antivenom treatment.
Whole IgG antivenom: An antivenom made from intact immunoglobulin G antibodies purified from immunized animals. This traditional format retains antibody regions that can contribute to reactions.
Antivenomics: A laboratory approach that measures which venom proteins are recognized by antivenom antibodies. It tests whether an antivenom binds the toxins present in a particular venom.
Antigen–antibody interaction: The specific binding between an antibody and the molecular target it recognizes. This binding can block toxins from interacting with their targets.
Vital Brazil: A Brazilian physician who developed specific antivenoms and founded the Butantan Institute. His research showed that antivenom effectiveness depends on the venom used to produce it.
Scorpion envenomation: Poisoning caused by toxins injected through a scorpion sting. Specific antivenoms are used for severe envenomation by some scorpion species.
F(ab')₂ antivenom: An antivenom made from antibody fragments that retain two toxin-binding arms but lack the Fc region. Its fragment format changes persistence and the risk profile compared with whole IgG.
Venom proteomics: The large-scale identification and analysis of proteins and peptides in animal venom. Mapping venom components can reveal toxins that current antivenoms fail to recognize.

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