Lectin

Lectins are carbohydrate-binding proteins that are highly specific for sugar groups that are part of other molecules, so cause agglutination of particular cells or precipitation of glycoconjugates and polysaccharides.

The selectivity of lectins means that they are useful for analyzing blood type, and they have been researched for potential use in genetically engineered crops to transfer pest resistance.

Several plant lectins have been found to recognize noncarbohydrate ligands that are primarily hydrophobic in nature, including adenine, auxins, cytokinin, and indole acetic acid, as well as water-soluble porphyrins.

[10] Lectin receptor kinases (LecRKs) are believed to recognize damage associated molecular patterns (DAMPs), which are created or released from herbivore attack.

[12] To avoid clearance from the body by the innate immune system, pathogens (e.g., virus particles and bacteria that infect human cells) often express surface lectins known as adhesins and hemagglutinins that bind to tissue-specific glycans on host cell-surface glycoproteins and glycolipids.

[17] Achylectins, isolated from Tachypleus tridentatus, show specific agglutinating activity against human A-type erythrocytes.

Anti-B agglutinins such as anti-BCJ and anti-BLD separated from Charybdis japonica and Lymantria dispar, respectively, are of value both in routine blood grouping and research.

The binding of lectins to cells in the digestive tract may disrupt the breakdown and absorption of some nutrients, and as they bind to cells for long periods of time, some theories hold that they may play a role in certain inflammatory conditions such as rheumatoid arthritis and type 1 diabetes, but research supporting claims of long-term health effects in humans is limited and most existing studies have focused on developing countries where malnutrition may be a factor, or dietary choices are otherwise limited.

He argued that lectins may damage a person's blood type by interfering with digestion, food metabolism, hormones, insulin production—and so should be avoided.

[23] D'Adamo provided no scientific evidence nor published data for his claims, and his diet has been criticized for making inaccurate statements about biochemistry.

[27][28][29] Lectins are one of many toxic constituents of many raw plants that are inactivated by proper processing and preparation (e.g., cooking with heat, fermentation).

Long before a deeper understanding of their numerous biological functions, the plant lectins, also known as phytohemagglutinins, were noted for their particularly high specificity for foreign glycoconjugates (e.g., those of fungi and animals)[35] and used in biomedicine for blood cell testing and in biochemistry for fractionation.

The earliest description of a lectin is believed to have been given by Peter Hermann Stillmark in his doctoral thesis presented in 1888 to the University of Dorpat.

Lateral hemagglutinine
An oligosaccharide (shown in grey) bound in the binding site of a plant lectin ( Griffonia simplicifolia isolectin IV in complex with the Lewis b blood group determinant); only a part of the oligosaccharide (central, in grey) is shown for clarity.
Lectin histochemistry of fish muscles infected by a myxozoan
Leucoagglutinin is a toxic phytohemagglutinin found in raw Vicia faba (fava bean).