Pattern Recognition in Legume Lectins to Extrapolate Amino Acid Variability to Sugar Specificity

Grandhi, Nisha Jayaprakash; Mamidi, Ashalatha Sreshty; Surolia, Avadhesha

doi:10.1007/978-3-319-11280-0_13

Cited by 5 publications

(6 citation statements)

References 64 publications

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“…Legume lectins display a large divergence in their carbohydrate specificity, and hence the residues in the carbohydrate binding domain are very variable. L-type lectins are involved in protein sorting in animals; their role in plants is not completely clear but they might be involved in immunity [ 32 ]. Despite the large variability, a few key amino acid residues are largely conserved among these lectins: an aspartate in the first loop, a glycine in the second loop, and an asparagine combined with an aromatic amino acid in the third loop [ 33 , 34 ].…”

Section: Resultsmentioning

confidence: 99%

The Distribution of Lectins across the Phylum Nematoda: A Genome-Wide Search

Bauters

Naalden

Gheysen

2017

IJMS

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Nematodes are a very diverse phylum that has adapted to nearly every ecosystem. They have developed specialized lifestyles, dividing the phylum into free-living, animal, and plant parasitic species. Their sheer abundance in numbers and presence in nearly every ecosystem make them the most prevalent animals on earth. In this research nematode-specific profiles were designed to retrieve predicted lectin-like domains from the sequence data of nematode genomes and transcriptomes. Lectins are carbohydrate-binding proteins that play numerous roles inside and outside the cell depending on their sugar specificity and associated protein domains. The sugar-binding properties of the retrieved lectin-like proteins were predicted in silico. Although most research has focused on C-type lectin-like, galectin-like, and calreticulin-like proteins in nematodes, we show that the lectin-like repertoire in nematodes is far more diverse. We focused on C-type lectins, which are abundantly present in all investigated nematode species, but seem to be far more abundant in free-living species. Although C-type lectin-like proteins are omnipresent in nematodes, we have shown that only a small part possesses the residues that are thought to be essential for carbohydrate binding. Curiously, hevein, a typical plant lectin domain not reported in animals before, was found in some nematode species.

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Section: Resultsmentioning

confidence: 99%

The Distribution of Lectins across the Phylum Nematoda: A Genome-Wide Search

Bauters

Naalden

Gheysen

2017

IJMS

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“…As presented in Figure , the monomer structure of kidney bean lectin (PHA-L, PDB number 1FAT), comprising two antiparallel sandwiched β-sheets, which are connected by α-turns, β-turns, and bends along with short loops, displays a jelly roll motif best described as a sandwich and contains two divalent cation metal-binding sites (Mn 2+ and Ca 2+ ) and a carbohydrate recognition domain (CRD). , The two antiparallel β-sheets constitute a flat six-strand “back” sheet, a concave seven-strand “front” sheet, and five short “top” β-sheets, which hold the two pieces together . Mn 2+ and Ca 2+ are not only necessary for the carbohydrate-binding activity of lectin, but also for functional conformation stability of the monosaccharide binding site, and they are also important for the hemagglutination activity. − Previously, when the kidney bean lectin was completely reacted with ethylenediaminetetraacetic acid (EDTA), the coagulation activity of the lectin was almost lost and the activity would be completely restored by re-addition of Ca 2+ and Mn 2+ . − Mg 2+ might have a substitution effect on the metal ions. , The CRD is a shallow depression located on the top surface of the dome-like structure, which can bind with both monosaccharides and oligosaccharides .…”

Section: Structure and Specificity Of Kidney Bean Lectinsmentioning

confidence: 99%

Detection of Lectin Protein Allergen of Kidney Beans (Phaseolus vulgaris L.) and Desensitization Food Processing Technology

Wang

Zhou

et al. 2021

J. Agric. Food Chem.

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With the increase of food allergy events related to not properly cooked kidney beans (Phaseolus vulgaris L.), more and more researchers are paying attention to the sensitization potential of lectin, one of the major storage and defensive proteins with the specific carbohydrate-binding activity. The immunoglobulin E (IgE), non-IgE, and mixed allergic reactions induced by the lectins were inducted in the current paper, and the detection methods of kidney bean lectin, including the purification strategies, hemagglutination activity, specific polysaccharide or glycoprotein interactions, antibody combinations, mass spectrometry methods, and allergomics strategies, were summarized, while various food processing aspects, such as the physical thermal processing, physical non-thermal processing, chemical modifications, and biological treatments, were reviewed in the potential of sensitization reduction. It might be the first comprehensive review on lectin allergen detection from kidney bean and the desensitization strategy in food processing and will provide a basis for food safety control.

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“…Legume lectins represent a crucial point in the study of the molecular basis of protein–carbohydrate interactions. Each has a CRD with a basic architecture accessible to both monosaccharides and/or oligosaccharides that confers remarkable divergence in their specificities [ 12 , 52 ]. Lectins can non-covalently interact with carbohydrates in a manner that is usually reversible and highly specific.…”

Section: Specificity Of Legume Lectinsmentioning

confidence: 99%

Legume Lectins: Proteins with Diverse Applications

Lagarda-Díaz

Guzmán-Partida

Vázquez–Moreno

2017

IJMS

140

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Lectins are a diverse class of proteins distributed extensively in nature. Among these proteins; legume lectins display a variety of interesting features including antimicrobial; insecticidal and antitumor activities. Because lectins recognize and bind to specific glycoconjugates present on the surface of cells and intracellular structures; they can serve as potential target molecules for developing practical applications in the fields of food; agriculture; health and pharmaceutical research. This review presents the current knowledge of the main structural characteristics of legume lectins and the relationship of structure to the exhibited specificities; provides an overview of their particular antimicrobial; insecticidal and antitumor biological activities and describes possible applications based on the pattern of recognized glyco-targets.

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Pattern Recognition in Legume Lectins to Extrapolate Amino Acid Variability to Sugar Specificity

Cited by 5 publications

References 64 publications

The Distribution of Lectins across the Phylum Nematoda: A Genome-Wide Search

The Distribution of Lectins across the Phylum Nematoda: A Genome-Wide Search

Detection of Lectin Protein Allergen of Kidney Beans (Phaseolus vulgaris L.) and Desensitization Food Processing Technology

Legume Lectins: Proteins with Diverse Applications

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