Is Lambs’ Blood Used to Make Antivenom?

Antivenom is a life-saving medical product administered to counteract the effects of envenomation from snakes, scorpions, and spiders. It is a biological product, meaning it is derived from living organisms, and its production process involves harnessing the natural immune response of an animal to create a therapeutic serum for humans. The concept is based on the body’s ability to produce specific proteins, known as antibodies, when exposed to a foreign substance like venom.

Clarifying the Source Animals

The idea that lambs’ blood is used to make antivenom stems from the fact that sheep are indeed one of the animals employed in modern production. While sheep are used by some manufacturers, large animals like horses remain the most common source animal globally due to their substantial blood volume and capacity to yield high quantities of plasma for processing. The size of a horse allows for the collection of significant amounts of hyperimmune plasma without compromising the animal’s health. Manufacturers also utilize other species, including goats, rabbits, camels, and llamas, depending on the specific product and regional production standards. The choice of animal is primarily a factor of logistics, antibody yield, and the subsequent purification steps that minimize the risk from foreign animal proteins.

How Antivenom Neutralizes Venom

Antivenom functions by introducing neutralizing antibodies, also called immunoglobulins, into the patient’s bloodstream to bind to the venom’s toxic components. Venom is a complex mixture of proteins and peptides designed to disrupt biological systems, such as the nervous system or blood clotting cascade. The goal of the antivenom antibodies is to render these toxins inert before they can cause widespread damage.

Neutralization occurs through a specific lock-and-key interaction where the antibody physically binds to the venom molecule (the antigen). This binding can directly block the toxin’s active site, preventing it from interacting with its target receptor on human cells. In other cases, the large size of the antibody complex creates a physical obstruction called steric hindrance, which blocks the venom from reaching its target. Once bound and neutralized, the resulting complex is safely cleared from the body by the immune system.

The Hyperimmunization Process

The process of generating high concentrations of specific antibodies begins with hyperimmunization, a controlled method of repeatedly exposing the host animal to a small, non-lethal dose of the target venom. This initial dose is often modified to reduce its toxicity, sometimes by chemically inactivating the venom to create a toxoid, ensuring the animal’s safety. The venom is usually administered along with an adjuvant, a substance that helps stimulate a stronger and more sustained immune response.

Over a period that can last several months to a year, the animal receives a series of booster injections, with the venom dose gradually increasing as the immune system builds tolerance. This regimen prompts the animal’s B-cells to produce large quantities of polyclonal antibodies, specifically Immunoglobulin G (IgG), which target the various toxins within the venom. Once antibody levels reach a high concentration, a plasma collection procedure is performed, which involves drawing blood and separating the plasma (the liquid component containing the antibodies) from the blood cells. The blood cells are then returned to the animal, allowing the process to be repeated while the animal is closely monitored.

From Raw Plasma to Usable Medicine

Raw plasma contains neutralizing antibodies, but also many other non-antibody proteins that can cause allergic reactions in humans, such as serum sickness. The manufacturing process therefore involves extensive purification to isolate the specific immunoglobulins and increase the safety profile of the final product. One common method is fractionation, which uses chemical agents like caprylic acid or ammonium sulfate to selectively precipitate and separate the IgG antibodies from the other plasma components.

Many modern antivenoms also undergo an enzymatic digestion step, where the whole IgG molecule is cleaved into smaller, more therapeutic fragments using enzymes like pepsin or papain. Pepsin digestion produces the F(ab’)2 fragment, a double-armed antibody fragment that retains its neutralizing capacity while eliminating the Fc region—the part of the antibody most likely to trigger adverse immune responses. Papain digestion yields the even smaller Fab (fragment antigen-binding) fragments. These smaller fragments penetrate tissues more effectively and are cleared from the body more rapidly, further reducing the risk of delayed allergic reactions.