A lectin was purified from the leaves of Allium altaicum and corresponding gene was cloned. The lectin namely Allium altaicum agglutinin (AAA) was ~24 kDa homodimeric protein and similar to a typical garlic leaf lectin. It was synthesized as 177 amino acid residues pre-proprotein, which consisted of 28 and 43 amino acid long N and C-terminal signal peptides, respectively. The plant expressed this protein more in scapes and flowers in comparison to the bulbs and leaves. Hemagglutination activity (with rabbit erythrocytes) was 1,428 fold higher as compared to Allium sativum leaf agglutinin (ASAL) although, the insecticidal activity against cotton aphid (Aphis gossypii) was relatively low. Glycan array revealed that AAA had higher affinity towards GlcAb1-3Galb as compared to ASAL. Homology analysis showed 57–94% similarity with other Allium lectins. The mature protein was expressed in E. coli as a fusion with SUMO peptide in soluble and biologically active form. Recombinant protein retained high hemagglutination activity.

Zubčević, N., M. Fočak and D. Suljević, 2018. Highly specifi c hemagglutination activity of plant lectins in specifi c species: case of Fabaceae and Solanaceae. Bulg. J. Agric. Sci., 24 (3): 391–397 Lectins are carbohydrate-binding proteins present in most of the plants and in some animals. They possess the ability to agglutinate erythrocytes with known carbohydrate specifi city since they have at least one non-catalytic domain that binds reversibly specifi c monosaccharides or oligosaccharides. This study investigated the presence of lectins in the plant species of the family Fabaceae and Solanaceae. The results of our study have shown that 6 of 10 plant lectins caused agglutination, and 4 of them did not cause agglutination of human erythrocytes. Blood agglutination activity against A, B, AB and 0 groups was shown after exposing blood to lectin extracts obtained from 80% of tested plants in family Fabaceae, and 20% of tested plants in family Solanaceae. The highest degree of agglu...

The legumes-Mucuna, Cowpea, Pigeon pea, African Yam Bean, Black-eyed pea, Soybean, Red kidney bean, Peanut, Green bean, and Bambara-were obtained from markets in Umuahia, ground in flour using Art's Way Roller Mill. Crude lectins were extracted from the milled legumes by soaking in distilled water for over 12 hours, followed by decanting; the proteins in the supernatant were precipitated by dissolving 10g of ammonium sulfate in 100ml of the supernatants. The crude lectin extracts were evaluated for hemagglutinin activity, using human erythrocytes. Mucuna lectins were specific for blood groups B + and AB +. Cowpea lectins agglutinated group A + and B +. African yam bean and Bambara lectins agglutinated all, while Pigeon pea was specific for groups A + , B + and O +. Mucuna cowpea, Pigeon pea, lectin was blood specific, while African yam bean and Bambara lectins were not. Lectins from Soybean, Black-eyed pea, and Green bean were blood group selective; while lectins from Kidney beans and Peanuts were pan-hemagglutinin lectins. Blood group O was less affected. Reduction in hemagglutinin activity was observed with a reduction in the concentration of the crude lectin extracts.

Lectins was extracted from processed and unprocessed black-eyed peas, green beans, soybeans, peanuts, and red kidney beans by grinding using attrition mill and then soaked in distilled water. The proteins in the supernatant were precipitated by dissolving 10g of ammonium sulphate in 100ml of the supernatants. The lectin extracts were evaluated for hemagglutinin activity using human erythrocytes from blood group A + , B + , AB + , and O + , respectively. Result revealed that lectins from unprocessed soybean, black-eyed pea and green bean are blood group selective and may be classified as blood type specific lectins. While lectins from kidney beans and peanuts agglutinated all blood groups and may be classified as panhemagglutinin lectins, i.e. they agglutinated erythrocytes from all blood groups. Result shows that blood group O is less affected by hemagglutinin activity of lectin. Reduction/loss of hemagglutinin activity was observed with reduction in concentration of the crude lectin extracts in all unprocessed legumes. Boiling (at 100 0 C) for 30minutes completely inactivated hemagglutinin activity of lectin in Black eyed peas, soybeans, green beans and red kidney beans. Slight hemagglutinin activity was seen in lectin from roasted peanuts, indicating that dry heating may be very effective method to inactivate lectin completely. Also, in this study, lectins were extracted from rice (Oryza sativa), maize (Zea mays), sorghum (Sorghum bicolor), Acha (Digitaria excells), millet (Panicum maniceum); partial purification of the extract assayed from hemugglutinin activity using 4% of human erythrocyte in lectin buffer. Extract from these selected cereals showed positive and negative agglutination reaction with blood group A + , B + , O + and AB + depending on the concentration (dilution) and the blood group. Lectin extract from maize showed no agglutination reaction when diluted in blood group A + , B + , and AB + and even when processed and diluted. While crude lectin extract from rice showed no activity in blood group A + , B + , and AB + and when unprocessed and showed lectin agglutination activity when processed by boiling (cooking) showing that heat may encourage its activity. Blood group B + , and AB + showed no activity in all dilution. Also acha showed high agglutination activity in blood group A + , B + , AB + and O + but losses activity in dilution a 2 and a 3. Crude lectin extract from processed sorghum showed