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Lectin

Molecular classification
Other (Carbohydrate-binding protein), Sometimes classed as "Receptor" or "Cell surface receptor" (for specific family members), Different structural families: C-type lectin, P-type lectin, Galectin (S-type), L-type, F-type, and others
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Overview

Lectin refers to a **large family of proteins**—not a single molecule or receptor—characterized by their ability to bind carbohydrates with high specificity[6][7]. Found in viruses, bacteria, plants, animals, and humans, lectins play diverse roles in cellular recognition, adhesion, and signaling[6][3]. They are structurally categorized based on their **carbohydrate recognition domains (CRDs)** into various families such as C-type, P-type, galectins, and others[1][6]. Biological functions include mediation of immune responses, opsonization, pathogen detection, and cell–cell communication[1][4]. Some lectins are potent toxins (e.g., ricin), while others serve as important biochemical tools, especially in glycoprotein research and diagnostics[7]. As a class, lectins are not considered **therapeutic targets**; individual lectin proteins may be, but "lectins" as a group is a **broad, unspecific target** and thus an incorrect or insufficiently granular entry for targeted drug discovery[6][7]. Caveat: "Lectins" is not a specific molecular target; information should be gathered and analyzed on a per-lectin basis (e.g., C-type lectin receptor, galectin-3), not for the superfamily as a whole[1][6][7].

Other names
Carbohydrate-binding protein
02

Mechanism of action

Agglutination of cells by crosslinking glycoproteins/glycolipids; Binding to specific carbohydrate structures, mediating biological recognition or toxic effects (e.g., ricin mechanism)

03

Biological functions

Cell–cell recognitionCell adhesionCell signalingImmune response (innate immunity, inflammation, pathogen recognition)Opsonization and phagocytosisActivation of complement pathwayEndocytosis and intracellular traffickingPlant defense and symbiosis
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Disease associations

Infection (host-pathogen interaction)InflammationCancer (diagnostics, not direct causation)Other (toxic agents like ricin can be lethal to cells)
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Safety considerations

Some lectins (e.g., ricin, abrin) are highly toxic and can inhibit protein synthesis, leading to cell deathPossible allergenicity and toxicity in food lectins
06

Biomarkers

Used in blood typing (lectins from *Dolichos biflorus*, *Ulex europaeus*, *Vicia graminea*, *Iberis amara*)Research tool for glycoprotein profiling

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