Lectiner

Lectiner is a term used in some languages to refer to proteins that, in English, are known as lectins. Lectins are a broad class of proteins or glycoproteins that bind specific carbohydrate structures. They occur in many organisms but are especially abundant in plants, where they are thought to play roles in defense against pests and pathogens and in seed germination and storage. Plant lectins typically recognize particular sugar motifs, such as galactose, mannose, or N-acetylglucosamine, and can bind multiple sugars, enabling them to cross-link glycoconjugates on cell surfaces or extracellular matrices.

Lectins vary in size, quaternary structure, and binding specificity. Some are soluble proteins, while others are bound to cell walls or membranes. A well-known property is their ability to cause agglutination of red blood cells in vitro, which historically aided their investigation.

Dietary lectins are most commonly discussed in the context of foods of plant origin, including legumes (for example beans and lentils), grains, and some seeds and vegetables. In humans, lectins can be resistant to digestion and may interact with gut lining, potentially causing irritation or interfering with nutrient absorption if consumed in large amounts in poorly prepared foods. Most edible lectins are deactivated by proper cooking, soaking, and fermentation; raw or inadequately processed legumes can trigger symptoms such as nausea or vomiting.

Beyond nutrition, lectins are used in laboratory techniques for glycan detection and separation, such as affinity chromatography and lectin histochemistry, and are studied for roles in cell signaling, immune modulation, and infectious disease.

Overall, lectins are a diverse and functionally varied group of carbohydrate-binding proteins. Their effects on health depend on the source, structure, dose, and preparation method, with most dietary lectins being of low risk when foods are properly prepared and diverse in a balanced diet. Note: the term lectiner appears in some languages as the equivalent of lectin.