Highly specifi c hemagglutination activity of plant lectins in specific species: case of Fabaceae and Solanaceae (original) (raw)
Related papers
International Journal of Research in Ayurveda & Pharmacy, 2013
Lectin from Erythrophleum suaveolens stem bark was partially purified and evaluated in terms of its haemagglutination activity. Ground, dried stem bark of Erythrophleum suaveolens was extracted by aqueous method and the protein extract was concentrated in 20-90 % saturation. The ammonium sulfate precipitate was subjected to gel filtration chromatography using Sephadex G-75 resin and fractions were tested for haemagglutination activity. The two fractions obtained with the highest hemmaglutinating activity were further subjected separately to ion-exchange chromatography using Sp-Sephadex C-50 resin. Isolated lectins were found to agglutinate chicken erythrocytes; fractions from gel filtration chromatography showed haemagglutinating activity of 0.1 HU/µL and 0.091 HU/µL, while the ion exchange fractions showed haemagglutinating activity of 0.05 HU/µL and all were stable at the temperature range of 30-60 0 C and pH range of 3-7. The carbohydrate content of the crude extract, Gel I, Gel II, Ion I and Ion II fractions were 0.04 %, 0.04 %, 0.03 %, 0.02 %, respectively. The crude and purified lectins inhibited agglutination in the presence of mannose and Nacetyl-glucoseamine sugars and showed five bands at positions 38kDa, 28kDa, 26kDa, 11kDa and 9kDa on a SDS-PAGE electrophoregram.
Hemagglutinin Activities of Lectin Extracts from Selected Legumes
Researchgate, 2020
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.
Biological Applications of Plants and Algae Lectins: An Overview
Carbohydrates - Comprehensive Studies on Glycobiology and Glycotechnology, 2012
Carbohydrates-Comprehensive Studies on Glycobiology and Glycotechnology 534 erythrocytes but not blood type B or O cells, whereas the extract of Lotus tetragonolobus agglutinated only blood type O erythrocytes [1,5]. The specific interaction between lectins and carbohydrates of erythrocytes played a crucial role in the investigations of the antigens associated with the ABO blood group system. In the subsequent decade, Morgan and Watkins found that the agglutination of type A erythrocytes by extracts of Phaseolus limensis was best inhibited by α-linked N-acetyl-Dgalactosamine, while the agglutination of O cells by the extract of L. tetragonolobus was best inhibited by α-linked L-fucose [6]. Around thirty years after Boyd, the research on lectins reached the molecular level studies. It was clear the need to a better understanding on the structural aspects of lectins. Then, in 1972 Edelman and colleagues established the primary sequence of ConA [6]. In the same year, Edelman's group and independently Karl Hardman with Clinton Ainsworth, solved the 3D structure of ConA by X-ray crystallography [7,8]. 2. What exactly is a lectin? In 1954 Boyd and Shapleigh proposed the term lectin, from the Latin verb legere (which means "to select"). This term was based on the fact that these proteins have the ability to distinguish between erythrocytes of different blood types [9]. Lectins were early defined as carbohydrate-binding proteins of nonimmune origin that agglutinate cells or as carbohydrate-binding proteins other than antibodies or enzymes. However, these definitions were updated, since some plant enzymes are fusion proteins composed of a carbohydrate-binding and a catalytic domain, for instance, type 2 RIPs, such as ricin and abrin, are fusion products of a catalytically active A-chain (which has the Nglycosidase activity) and a carbohydrate-binding B-chain, both linked by a disulfide bond [10]. Furthermore, there is in nature carbohydrate-binding proteins possessing only one binding site and, therefore, are not capable of precipitating glycoconjugates or agglutinating cells [11]. Thus, in 1995 Peumans and Van Damme proposed the most suitable definition for lectins. According to the "new" definition, all plant proteins that possess at least one noncatalytic domain that binds reversibly to a specific mono-or oligosaccharide are considered as lectins [12,13]. 2.1. Plant lectins Lectins are proteins widely distributed in nature such in microorganisms, plants, animals and humans, acting as mediators of a wide range of biological events that involve the crucial step of protein-carbohydrate recognition, such as cell communication, host defense, fertilization, cell development, parasitic infection, tumor metastasis, inflammation, etc [14-15]. Peumans and Van Damme classified the plant lectins according to their overall structure. Merolectins consist exclusively of a single carbohydrate-binding domain (e.g. hevein, a Biological Applications of Plants and Algae Lectins: An Overview 535 chitin-binding latex protein isolated from the rubber tree Hevea brasiliensis). Since merolectins have a unique carbohydrate-binding site, they are incapable of precipitating glycoconjugates or agglutinating cells. Hololectins are also built of carbohydrate-binding domains. However, they contain at least two such domains that are identical or very similar. Because these lectins are di-or multivalent they can agglutinate cells and/or precipitate glycoconjugates. Most plant lectins are hololectins. Superlectins are built of at least two carbohydrate-binding domains. Unlike hololectins, these domains are not identical or similar. Thus, superlectins recognize structurally different sugar (e.g. TxLCI, a tulip bulb lectin that recognizes mannose and N-acetyl-galactosamine). Chimerolectins are fusion proteins that consist of two different chains, one of them with a remarkable catalytic activity (or another biological activity). RIPs type 2 are examples of chimerolectins [11-12].
APPLICATIONS OF PLANT LECTINS IN BIOTECHNOLOGY AND THERAPEUTICS: Plant lectins application
The Journal of Microbiology, Biotechnology and Food Sciences, 2021
Lectins are carbohydrate-binding proteins broadly used in various therapeutic and biomedical applications. The variable affinity of lectins towards variety of carbohydrates has raised attention for the biologist to explore functional aspects of lectins. Lectins express specificity to simple carbohydrates for example mannose, lactose, sialic acid, complex glycan, and glycoproteins. Lectins are classified based on their sugar specificity and are used as a tool to study protein-carbohydrate interactions. Lectins are ubiquitous in nature and identified from all sources such as bacteria, fungi, algae, and animals. Plants are the most abundant source of lectins, and till now, more than three hundred lectins were characterized from plants. These are distributed to various parts of a plant according to their requirements and function. The physiological role of lectins in a plant is still not well understood. The overabundant presence of lectins in plant seeds and storage tissues indicated their role in plant development. Plant lectins shows a broad range of activities like antibacterial, antifungal, insecticidal, anticancerous, antileishmanial, antiviral, and anticoagulants. In this review, we aim to highlight the plant lectins classification and their application in various biological aspects. ARTICLE INFO
Identification and Characterization of Lectins from Leguminosae Plants
https://www.ijhsr.org/IJHSR\_Vol.9\_Issue.2\_Feb2019/IJHSR\_Abstract.017.html, 2019
Introduction: Since lectins are widely found in Leguminosae family due to their high protein content, in the present study, an attempt has been made to identify such legume lectins which have the agglutination properties with the red blood cells from normal individuals. Methods: Normal blood samples were collected, using the finger-prick technique. All blood samples were washed thrice in physiological saline and re-suspended at a concentration of 2% in normal saline. For ABO typing, standard serological procedure were followed. Results: In the results, various lectins showed the hemagglutination reaction pattern with human ABO blood groups. The lectin reacted with various blood groups with the strength of 1:1, 1:2, 1:4, 1:8, 1:16, 1:32, 1:64, and 1:128. Conclusion: The research findings were considered as the first step towards the field of sports nutrition. The lectin seeds are collected from the daily routine of the sports person, without knowing the effect of seeds on the body. Properly denaturized seeds should be consumed.
Plant Lectins: Biochemical Characterization and Function
2013
The present paper is dedicated to plant lectins, their classifi cation, molecular structure, distribution in different plant organs and involvement in such biological functions as: cell to cell communication, phytoimmunity, symbiotic relationships, also cytotoxic action, mitogenic activity and participation in the immune reactions (system of complement). The future use of lectins in medical practice has been considered.
Structure-function and application of plant lectins in disease biology and immunity
Food and Chemical Toxicology, 2019
Lectins are proteins with a high degree of stereospecificity to recognize various sugar structures and form reversible linkages upon interaction with glyco-conjugate complexes. These are abundantly found in plants, animals and many other species and are known to agglutinate various blood groups of erythrocytes. Further, due to the unique carbohydrate recognition property, lectins have been extensively used in many biological functions that make use of protein-carbohydrate recognition like detection, isolation and characterization of glycoconjugates, histochemistry of cells and tissues, tumor cell recognition and many more. In this review, we have summarized the immunomodulatory effects of plant lectins and their effects against diseases, including antimicrobial action. We found that many plant lectins mediate its microbicidal activity by triggering host immune responses that result in the release of several cytokines followed by activation of effector mechanism. Moreover, certain lectins also enhance the phagocytic activity of macrophages during microbial infections. Lectins along with heat killed microbes can act as vaccine to provide long term protection from deadly microbes. Hence, lectin based therapy can be used as a better substitute to fight microbial diseases efficiently in future.
Applications of Plant Lectins in Biotechnology and Therapeutics
2021
Lectins are carbohydrate-binding proteins broadly used in various therapeutic and biomedical applications. The variable affinity of lectins towards variety of carbohydrates has raised attention for the biologist to explore functional aspects of lectins. Lectins express specificity to simple carbohydrates for example mannose, lactose, sialic acid, complex glycan, and glycoproteins. Lectins are classified based on their sugar specificity and are used as a tool to study protein-carbohydrate interactions. Lectins are ubiquitous in nature and identified from all sources such as bacteria, fungi, algae, and animals. Plants are the most abundant source of lectins, and till now, more than three hundred lectins were characterized from plants. These are distributed to various parts of a plant according to their requirements and function. The physiological role of lectins in a plant is still not well understood. The overabundant presence of lectins in plant seeds and storage tissues indicated their role in plant development. Plant lectins shows a broad range of activities like antibacterial, antifungal, insecticidal, anticancerous, antileishmanial, antiviral, and anticoagulants. In this review, we aim to highlight the plant lectins classification and their application in various biological aspects. ARTICLE INFO
Screening and Partial Purification of Lectin from Various Bangladeshi Plant Seeds
American Journal of Sensor Technology, 2014
Lectins are group of proteins or glycoprotein of non immunological origins, which can recognize specific carbohydrate structure. In this research work hemaggulutination was used as technique for screening Bangladeshi vegetables for lectin. Five varieties of legume plant seeds Canavalia gladiata(Sword bean),Lens culinaris (Moshordal), Peasum sativam (Motorsuti), Vigna unguiculata subsp. sesquipedalis (Borboti), Cajanus cajan (Arhordal), one Amaranthaceae Amaranthus caudate (katoadata) and one fruit Citrullus lanatus (Watermelon) species from Bangladesh were examined for lectins with chicken and human erythrocytes. Crude extracts from all the species showed agglutinating activity against the erythrocytes used. The lowest protein concentration required to produce erythrocytes agglutination varied remarkable ranging from 0.7 µg/ml to 8080 µg/ml. The strongest activities were shown in the agglutination of human blood erythrocytes by partial purification of lectin from Moshordal and chick...
Journal of Pharmaceutical Research International, 2021
Lectin has various physiological roles in cell agglutination, based on their carbohydrate-binding properties, plant lectins are widely used for the detection, segregation, and characterization of glycoconjugates. Rhesus (Rh) factor is a protein that is inherited and found on the surface of red blood cells. If the surface protein is present, the RBC is Rh positive; otherwise, it is Rh-negative in nature. In this paper, we use agglutination reactions to investigate the effect of different cold and hot water extracted plants on RBC antigens as an alternative to commercial monoclonal antibodies. Extensive research on the sequence homology and 3-D structure of various plant lectins suggests that they have been conserved throughout evolution and may play important physiological roles that are still unknown.