Prevalence, biological activity and genetic manipulation of lectins in foods

doi:10.1016/0924-2244(96)10015-7

Trends in Food Science & Technology

Volume 7, Issue 4, April 1996, Pages 132-138

https://doi.org/10.1016/0924-2244(96)10015-7 Get rights and content

Abstract

Many food plants contain proteins that are usually referred to as lectins on the basis of their specific carbohydrate-binding properties. Some of these lectins protect the plant against predatory invertebrates and higher animals, and they may also be harmful to humans. Therefore, the presence of lectins in food plants and foodstuffs is an important issue in food science. Although the risks of acute toxicity are low, prolonged exposure to low levels of lectins may be harmful to human health. Hence, the introduction of foreign lectin genes into food plants should be restricted to those lectins that are harmless to humans. Elimination of lectins from crop plants using breeding programmes or genetic engineering should, in principle, be achievable in the case of some important legumes.

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Cited by (62)

Glycan-directed SARS-CoV-2 inhibition by leek extract and lectins with insights into the mode-of-action of Concanavalin A
2024, Antiviral Research
Four years after its outbreak, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) remains a global challenge for human health. At its surface, SARS-CoV-2 features numerous extensively glycosylated spike proteins. This glycan coat supports virion docking and entry into host cells and at the same time renders the virus less susceptible to neutralizing antibodies. Given the high genetic plasticity of SARS-CoV-2 and the rapid emergence of immune escape variants, targeting the glycan shield by carbohydrate-binding agents emerges as a promising strategy. However, the potential of carbohydrate-targeting reagents as viral inhibitors remains underexplored. Here, we tested seven plant-derived carbohydrate-binding proteins, called lectins, and one crude plant extract for their antiviral activity against SARS-CoV-2 in two types of human lung cells: A549 cells ectopically expressing the ACE2 receptor and Calu-3 cells. We identified three lectins and an Allium porrum (leek) extract inhibiting SARS-CoV-2 infection in both cell systems with selectivity indices (SI) ranging between >2 and >299. Amongst these, the lectin Concanavalin A (Con A) exerted the most potent and broad activity against a panel of SARS-CoV-2 variants. We used multiplex super-resolution microscopy to address lectin interactions with SARS-CoV-2 and its host cells. Notably, we discovered that Con A not only binds to SARS-CoV-2 virions and their host cells, but also causes SARS-CoV-2 aggregation. Thus, Con A exerts a dual mode-of-action comprising both, antiviral and virucidal, mechanisms. These results establish Con A and other plant lectins as candidates for COVID-19 prevention and basis for further drug development.
OdTx12/GNA, a chimeric variant of a β excitatory toxin from Odontobuthus doriae, reveals oral toxicity towards Locusta migratoria and Tenebrio molitor
2021, Toxicon
OdTx12, a beta excitatory toxin from Odontobothus doriae had previously been identified and characterized. It had been shown that OdTx12 causes significant lethal effects on insects by injection but does not show any toxicity on mice. Due to the natural ineffectiveness of scorpion toxins to act as oral toxins, OdTx12 was fused to Galanthus nivalis agglutinin (GNA), a protein with the potential to cross the insect gut. The sequence of OdTx12/GNA gene was chemically synthesized, cloned in Escherichia coli, and expressed. The effect of the purified fusion protein (OdTx12/GNA) was assessed on the insect and mammalian cell lines, insect larvae and mice. Toxicity assay on insect cell culture (SF9 cell line) showed comparable toxicity between OdTx12 and OdTx12/GNA (LD50 of 0.0030 and 0.0048 μM, respectively). Also very similar mortality rates were observed by injecting OdTx12 and OdTx12/GNA to Locusta migratoria and Tenebrio molitor. Oral administration of OdTx12/GNA, after five days of feeding, resulted in 96.6% and 98.3% mortality of L. migratoria and T. molitor larvae with an LC50 of 0.69 and 0.43 nmol/g of insect food, respectively, while OdTx12 alone did not cause any toxic effects on the larvae orally, suggesting the role of GNA in delivering the toxin to the insect's haemolymph. No toxicity or mortality was observed after toxicity testing of OdTx12/GNA on a mammalian cell line (HEP-2) or any mortality in vivo, by testing the protein in the laboratory mouse.
Herein, we demonstrated that the fusion protein OdTx12/GNA could be considered an effective toxin for the biological control of insects.
Reverse micellar extraction of lectin from black turtle bean (Phaseolus vulgaris): Optimisation of extraction conditions by response surface methodology
2015, Food Chemistry
Lectin from black turtle bean (Phaseolus vulgaris) was extracted and purified by reverse micellar extraction (RME) method. Response surface methodology (RSM) was used to optimise the processing parameters for both forward and backward extraction. Hemagglutinating activity analysis, SDS–PAGE, RP-HPLC and FTIR techniques were used to characterise the lectin. The optimum extraction conditions were determined as 77.59 mM NaCl, pH 5.65, AOT 127.44 mM sodium bis (2-ethylhexyl) sulfosuccinate (AOT) for the forward extraction; and 592.97 mM KCl, pH 8.01 for the backward extraction. The yield was 63.21 ± 2.35 mg protein/g bean meal with a purification factor of 8.81 ± 0.17. The efficiency of RME was confirmed by SDS–PAGE and RP-HPLC, respectively. FTIR analysis indicated there were no significant changes in the secondary protein structure. Comparison with conventional chromatographic method confirmed that the RME method could be used for the purification of lectin from the crude extract.
Phytohemagglutinins augment red kidney bean (Phaseolus vulgaris L.) induced allergic manifestations
2013, Journal of Proteomics
Citation Excerpt :
The allergic potential of several leguminous foods including peanut, soybean, lupin, lentil, chickpea, red gram and green gram has been explored [3]. The presence of lectins in foodstuffs is an important health concern which may induce acute toxicity and its chronic exposure leads to harmful consequences to human health [25]. These dietary lectins are protein that bind to surface glycoproteins (or glycolipids) on erythrocytes or lymphocyte membranes and may function as allergens as well as hemagglutinating agents [26].
Red kidney bean (Phaseolus vulgaris L.), a commonly consumed bean has been reported to induce allergic reactions in susceptible individuals. Phytohemagglutinins (PHAs, mainly PHA-P) contribute a major proportion of red kidney bean seeds. However, their roles in red kidney bean induced allergic reactions are still to be explored. This study was carried out to understand the role of PHAs in allergic manifestations using BALB/c mice and cultures of splenocyte, RBL-2H3 cells as well as bone marrow mast cells (BMMCs). Also, the characterization of allergic components from PHA-P was studied by LC-MS/MS. Enhanced levels of specific IgE and IgG1, clinical scores, cytokines and chemokines, β-hexosaminidase, histamine, cysteinyl leukotriene, prostaglandin D₂ and abrupt histological changes in the intestine, lung and spleen indicated a pivotal role of PHA-P in red kidney bean allergy. Further, LC-MS/MS study revealed two IgE binding components of PHA-P as PHA-L and PHA-E. Enhanced specific IgE/IgG1 and β-hexosaminidase level elucidated the possible role of PHA-L and PHA-E in allergic manifestations. Furthermore, in the presence of IgE inhibitor piceatannol, reduced β-hexosaminidase release to some extent was noticed. The up regulated expression of GATA-3 and T-bet expression was observed in PHA-L as well as PHA-E groups. Taken together, this study revealed the fact that allergenicity potential of red kidney bean may get augmented due to the presence of different phytohemagglutinins.
Although food allergy is an immune provocation induced mainly by dietary allergenic protein components of the food, the role of dietary lectins in the food induced allergic manifestations cannot be ruled out. Here we provide the systematic evidences about the allergenic potential of PHAs and further disclosed the culprit components as PHA-L and PHA-E. It is an important finding that the PHA-L and PHA-E can cause allergic manifestations via not only the IgE mediated pathway but also the non-IgE mediated allergic reactions as evident by the Th1/Th2 cytokines and transcription factors. Further, the PHA-L seems to be more allergenic than the PHA-E. This article is part of a Special Issue entitled: Translational plant proteomics.
High doses of gamma radiation suppress allergic effect induced by food lectin
2013, Radiation Physics and Chemistry
Citation Excerpt :
During one week, mice were treated for seven consecutive days: Non-immunized control animals were treated with 1 mL saline/day; Immunized mice were treated with 1 mL saline/day; Immunized mice were treated with non-irradiated Cramoll; and immunized mice were treated with irradiated Cramoll at 1, 10 and 25 kGy, respectively. The dose of bean lectin (27 mg/kg body weight)/day) was according to the total dietary intake of lectins in human subjects consuming vegetarian diets (calculations based on data from Peumans and Van Damme, 1996). Body weight was determined before and after immunization and oral treatment.
One of the most promising areas for the development of functional foods lies in the development of effective methods to reduce or eliminate food allergenicity, but few reports have summarized information concerning the progress made with food irradiation. In this study, we investigated the relationship between allergenicity and molecular structure of a food allergen after gamma irradiation and evaluate the profile of the allergic response to irradiated allergens. Cramoll, a lectin isolated from a bean and used as a food allergen, was irradiated and the possible structural changes were accompanied by spectrofluorimetry, circular dichroism and microcalorimetry. Subsequently, sensitized animals subjected to intragastric administration of non-irradiated and irradiated Cramoll were treated for 7 days. Then, body weight, leukocytes, cytokine profiles and histological parameters were also determined. Cramoll showed complete inhibition of intrinsic activity after high radiation doses. Changes in fluorescence and CD spectra with a simultaneous collapse of the tertiary structure followed by a pronounced decrease of native secondary structure were observed after irradiation. After oral challenge, sensitized mice demonstrate an association between Cramoll intake, body weight loss, eosinophilia, lymphocytic infiltrate in the gut and Eotaxin secretion. Irradiation significantly reduces, according to the dose, the effects observed by non-irradiated food allergens. We confirm that high-dose radiation may render protein food allergens innocuous by irreversibly compromising their molecular structure.
Low-dose gamma irradiation of food protein increases its allergenicity in a chronic oral challenge
2013, Food and Chemical Toxicology
Citation Excerpt :
During 28 days, mice were treated as follows: group A, immunized mice were treated with 1 mL saline/day; group B, immunized mice were treated with non-irradiated Con-A; group C and D immunized mice were treated with irradiated Con-A at 1 and 25 kGy, respectively. The dose of bean lectin (27 mg/kg body weight/day) was according to total dietary intake of lectins in human subjects consuming vegetarian diets – calculations based on data from Peumans and van Damme (1996). Body weight was determined before and after immunization and after oral challenge.
Few chronic food protein models have described the relationship between allergenicity and the molecular structure of food protein after physical processing. The effect of γ-radiation on the structure of food protein was measured by fluorescence, circular dichroism and microcalorimetry. BALB/c mice were intraperitoneally sensitized and then given non-irradiated and irradiated Con-A by daily gavage for 28 days. The tendency to form insoluble amorphous aggregates and partially unfolded species was observed after irradiation. The administration of non-irradiated and irradiated samples at low-dose significantly increased weight loss as well as plasma levels of eotaxin in animals repeatedly exposed to Con-A. Significant lymphocytic infiltrate filling completely the stroma of microvilli and tubular glands was observed in the small intestinal of the group given Con-A irradiated at a low dose. This phenotype was not observed in animals treated with Con-A irradiated at a high dose.

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Trends in Food Science & Technology

Abstract

References (29)

Ribosome-inactivating Proteins from Plants

Biochim. Biophys. Acta

Lectins in the United States Diet: A Survey of Lectins in Commonly Consumed Foods and a Review of the Literature

Am. J. Clin. Nutr.

Nutritional Significance of Lectins in the Diet

Secondary Metabolites in Plant Defence Mechanisms

New Phytol.

Plant Defensins: Novel Antimicrobial Peptides as Components of the Host Defense System

Plant Physiol.

Protease Inhibitors in Plants: Genes for Improving Defenses Against Insects and Pathogens

Annu. Rev. Phytopathol.

The Role of Lectins in Plant Defense

Histochem. J.

The Mannose Binding Monocot Lectins and Their Genes' in Lectins, Biomedical Perspectives

Nutritional Evaluation of Kidney Beans (Phaseolus vulgaris; The Toxic Principle

J. Sci. Food Agric.

The Relationship Between Survival and Binding of Plant Lectins During Small Intestinal Passage and Their Effectiveness as Growth Factors

Digestion

‘Phaseolus vulgaris’ Lectin Induces Growth and Increases the Polyamine Content of Rat Small Intestine in vivo

Med. Sci. Res.

Antinutritive Effects of Wheat Germ Agglutinin and Other N-Acetylglucosamine Specific Lectins

Br. J. Nutr.

Plant Lectins

Lectins as Plant Defense Proteins

Plant Physiol.

Cited by (62)

Glycan-directed SARS-CoV-2 inhibition by leek extract and lectins with insights into the mode-of-action of Concanavalin A

OdTx12/GNA, a chimeric variant of a β excitatory toxin from Odontobuthus doriae, reveals oral toxicity towards Locusta migratoria and Tenebrio molitor

Reverse micellar extraction of lectin from black turtle bean (Phaseolus vulgaris): Optimisation of extraction conditions by response surface methodology

Phytohemagglutinins augment red kidney bean (Phaseolus vulgaris L.) induced allergic manifestations

High doses of gamma radiation suppress allergic effect induced by food lectin

Low-dose gamma irradiation of food protein increases its allergenicity in a chronic oral challenge

ReviewPrevalence, biological activity and genetic manipulation of lectins in foods

Abstract

Biochim. Biophys. Acta

Am. J. Clin. Nutr.

Secondary Metabolites in Plant Defence Mechanisms

New Phytol.

Plant Defensins: Novel Antimicrobial Peptides as Components of the Host Defense System

Plant Physiol.

Protease Inhibitors in Plants: Genes for Improving Defenses Against Insects and Pathogens

Annu. Rev. Phytopathol.

The Role of Lectins in Plant Defense

Histochem. J.

The Mannose Binding Monocot Lectins and Their Genes' in Lectins, Biomedical Perspectives

Nutritional Evaluation of Kidney Beans (Phaseolus vulgaris; The Toxic Principle

J. Sci. Food Agric.

The Relationship Between Survival and Binding of Plant Lectins During Small Intestinal Passage and Their Effectiveness as Growth Factors

Digestion

‘Phaseolus vulgaris’ Lectin Induces Growth and Increases the Polyamine Content of Rat Small Intestine in vivo

Med. Sci. Res.

Antinutritive Effects of Wheat Germ Agglutinin and Other N-Acetylglucosamine Specific Lectins

Br. J. Nutr.

Plant Lectins

Lectins as Plant Defense Proteins

Plant Physiol.

Review
Prevalence, biological activity and genetic manipulation of lectins in foods