scholarly journals Plant lectins and their many roles: Carbohydrate-binding and beyond

2021 ◽  
pp. 153531
Author(s):  
Sushma Naithani ◽  
Sneha Sudha Komath ◽  
Arthur Nonomura ◽  
Govindjee Govindjee
Keyword(s):  
Carbohydrate Binding ◽  
Plant Lectins

scholarly journals Effects of Plant Lectins on Human Erythrocyte Agglutination

2016 ◽  
Vol 17 (3) ◽  
pp. 207-214 ◽  
Author(s):  
Nadja Zubcevic ◽  
Suljevic Damir ◽  
Muhamed Focak ◽  
Dunja Rukavina
Keyword(s):  
Plant Species ◽  
Plant Extracts ◽  
Human Erythrocyte ◽  
Binding Proteins ◽  
Carbohydrate Binding ◽  
Plant Lectins ◽  
Blood Types ◽  
The Family ◽  
Carbohydrate Binding Proteins

AbstractPlant lectins are carbohydrate binding proteins or phytohaemagglutinins present in most plants, especially seeds and tubers, which include cereals, potatoes and beans. Lectins have great significance in the diet because of their involvement in gastrointestinal difficulties and erythrocyte agglutination. Blood agglutination activity against A, B, AB and O groups was shown after exposing blood to extracts obtained from 55% of tested plants, while in 45% of plants, agglutination was absent. The results of our study have shown that in humans, 40% of plant extracts exhibited activity against A, 40% of plant extracts exhibited activity against B, and 50% of plant extracts exhibited activity against AB and O groups in humans. The concentration of plant lectins depends on the part of the plant. Lectins from the seeds of certain plants cause the greatest percentage of erythrocyte agglutination, while the lowest agglutination was caused by plant bulbs and leaves. However, lectins derived from all plant species of the family Fabaceae agglutinated erythrocytes of all blood types to some extent.

A novel mannose-binding lectin from Liparis nervosa with anti-fungal and anti-tumor activities

2020 ◽  
Vol 52 (10) ◽  
pp. 1081-1092
Author(s):  
Na Jiang ◽  
Yuqing Wang ◽  
Jing Zhou ◽  
Ruxiao Zheng ◽  
Xiao Yuan ◽  
...  
Keyword(s):  
Gel Filtration ◽  
Sclerotium Rolfsii ◽  
Exchange Chromatography ◽  
Mannose Binding Lectin ◽  
Carbohydrate Binding ◽  
Plant Lectins ◽  
Mannose Binding ◽  
Anti Fungal ◽  
Binding Lectin

Abstract Plant lectins are carbohydrate-binding proteins with nonimmune origin, which can reversibly bind with carbohydrates, agglutinate cells, and precipitate polysaccharides and glycoconjugates. Plant lectins have attracted much attention for their anti-virus, anti-proliferation, and pro-apoptosis properties. Thus the exploration of new lectins has received special attention. Here we purified a mannose-binding lectin from the rhizomes of Liparis nervosa by ion exchange chromatography on DEAE-Sepharose, affinity chromatography on Mannose-Sepharose 4B, and gel filtration chromatography on Sephacryl S-100. The purified L. nervosa lectin (LNL) was identified to be a monomeric protein with a molecular mass of 13 kDa. LNL exhibited hemagglutinating activity towards rabbit erythrocytes, and its activity could be strongly inhibited by D-mannose, N-acetyl glucosamine and thyroglobulin. In vitro experiments showed that LNL exhibited a comparable anti-fungal activity against Piricularia oryzae (Cavara), Bipolaris maydis, Fusarium graminearum, and Sclerotium rolfsii, and anti-proliferation activity against tumor cells by inducing apoptosis. The full-length cDNA sequence of LNL is 715 bp in length and contains a 525 bp open reading frame (ORF) encoding a 110-residue mature protein. It was predicted to have three mannose-binding conserved motifs ‘QXDXNXVXY’. The binding pattern of LNL was further revealed by homology modeling and molecular docking. We demonstrated that LNL is not only a potential therapeutic candidate against tumor but also a new anti-fungal agent.

Lectins Are the Sparkle of Hope for Combating Coronaviruses and the Global COVID 19

2021 ◽  
Author(s):  
Heba S. Abbas ◽  
Muddukrishnaiah K
Keyword(s):  
T Lymphocyte ◽  
Higher Plants ◽  
Research Work ◽  
Scientific Work ◽  
Carbohydrate Binding ◽  
Structural Genomic ◽  
Plant Lectins ◽  
Genomic Variations ◽  
Binding Agents ◽  
Human Coronaviruses

Today the crisis of coronavirus disease 2019 (COVID-19) pandemic represents a threat worldwide because it is a leading cause of human morbidity and mortality. Besides, it possesses a destroying impact on countries’ economies. Therefore, there is an urgent need for hard research work and global collaboration to find a potential therapy. In this review, structural genomic variations in COVID 19 and further therapeutic options of Coronaviridae family or COVID 19 are expressed. Lectins are natural proteins, which can exist in algae, higher plants, banana, actinomycetes, fungi, and archaea, and they have antiviral properties. Griffithsin lectin, isolated from red algae, has noteworthy efficacy against lethal SARS-CoV infection, human coronaviruses, and other animal coronaviruses. Furthermore, all mannose-specific plant lectins have anti-coronaviruses properties except for garlic lectins. However, lectins from mushrooms can act as immunomodulators by activating T-lymphocyte or stimulating dendrites or cytokines. The lectin may hinder glucans on viral spike protein and prevent entry and the virus's release. Lectin's anti-coronavirus activities include a glimmer of hope to tackle the global COVID 19 crisis and inspire more scientific work on carbohydrate-binding agents against SARS-CoV-2.

scholarly journals Can Plant Lectins Help to Elucidate Insect Lectin-Mediated Immune Response?

Insects ◽  
2021 ◽  
Vol 12 (6) ◽  
pp. 497
Author(s):  
Pengyu Chen ◽  
Kristof De Schutter ◽  
Els J. M. Van Damme ◽  
Guy Smagghe
Keyword(s):  
Immune Responses ◽  
Control Strategies ◽  
Insect Immunity ◽  
Carbohydrate Binding ◽  
Immunomodulatory Effects ◽  
Plant Lectins ◽  
Range Of Functions ◽  
Global Understanding ◽  
Carbohydrate Binding Proteins ◽  
Specific Sugar

Lectins are carbohydrate-binding proteins that recognize and selectively bind to specific sugar structures. This group of proteins is widespread in plants, animals, and microorganisms, and exerts a broad range of functions. Many plant lectins were identified as exogenous stimuli of vertebrate immunity. Despite being the largest and most diverse taxon on earth, the study of lectins and their functions in insects is lagging behind. In insects, research on lectins and their biological importance has mainly focused on the C-type lectin (CTL) family, limiting our global understanding of the function of insect lectins and their role in insect immunity. In contrast, plant lectins have been well characterized and the immunomodulatory effects of several plant lectins have been documented extensively in vertebrates. This information could complement the missing knowledge on endogenous insect lectins and contribute to understanding of the processes and mechanisms by which lectins participate in insect immunity. This review summarizes existing studies of immune responses stimulated by endogenous or exogenous lectins. Understanding how lectins modulate insect immune responses can provide insight which, in turn, can help to elaborate novel ideas applicable for the protection of beneficial insects and the development of novel pest control strategies.

scholarly journals Studies on Lectin Mediated Agglutination Reaction on Red Blood Cell Surface Antigens Using Hot and Cold Water Plant Extracts

2021 ◽  
pp. 48-52
Author(s):  
Bhavya Sahithi Velagapudi ◽  
Hemanth Sai Nannapaneni ◽  
Akanksha Alampally ◽  
Suryanarayana Veeravilli ◽  
Duggipogu Praveen Kumar ◽  
...  
Keyword(s):  
Cold Water ◽  
Surface Protein ◽  
Hot Water ◽  
Carbohydrate Binding ◽  
Cell Surface Antigens ◽  
Binding Properties ◽  
Cell Agglutination ◽  
Plant Lectins ◽  
Water Plant

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.

Aphid Feeding on Plant Lectins Falling Virus Transmission Rates: A Multicase Study

2020 ◽  
Vol 113 (4) ◽  
pp. 1635-1639
Author(s):  
Frederic Francis ◽  
Julian Chen ◽  
Liu Yong ◽  
Emilie Bosquee
Keyword(s):  
Acyrthosiphon Pisum ◽  
Barley Yellow Dwarf Virus ◽  
Crop Protection ◽  
Virus Transmission ◽  
Blocking Agent ◽  
Plant Viruses ◽  
Carbohydrate Binding ◽  
Lower Efficiency ◽  
Plant Lectins ◽  
Yellow Dwarf Virus

Abstract Aphids are insect vectors that have piercing–sucking mouthparts supporting diversified patterns of virus–vector interactions. Aphids primarily retain circulative viruses in the midgut/hindgut, whereas noncirculative viruses tend to be retained in the stylet. Most viruses, and many proteins from animals, have carbohydrate or carbohydrate-binding sites. Lectins vary in their specificity, of which some are able to bind to viral glycoproteins. To assess the potential competition between lectins and viral particles in virus transmission by aphids, this study examined how feeding plant lectins to aphids affects the transmission efficiency of viruses. Sitobion avenae (F, 1794) (Homoptera: Aphididae) aphids fed with Pisum sativum lectin (PSL) transmitted Barley yellow dwarf virus with significantly lower efficiency (four-fold ratio). Pea enation mosaic virus was significantly reduced in Acyrthosiphon pisum Harris (Homoptera: Aphididae) aphids fed with the lectin Concanavalin A. In comparison, the transmission of Potato virus Y was significantly reduced when Myzus persicae Sultzer (Homoptera: Aphididae) aphids were fed with PSL. Thus, lectin could be used as a blocking agent of plant viruses, facilitating an alternative approach for crop protection.

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