Lectin Sequences Research Articles

Identification and Functional Analysis of a Novel L-Type Lectin (NdLTL1) from Neocaridina denticulata sinensis.

This study investigates an L-type lectin, NdLTL1, derived from Neocaridina denticulata sinensis, emphasizing its role in immune defense through carbohydrate binding and bacterial agglutination. Bioinformatics analysis identified 179 lectin sequences, leading to subsequent investigations into the structure and function of NdLTL1. The open reading frame (ORF) of NdLTL1 spans 966 bp and encodes a protein consisting of 321 amino acids (36.25 kDa), which features a signal peptide, a transmembrane domain and Lectin_leg-like domain. Three-dimensional modeling revealed three antiparallel β-sheets characteristic of Lectin_leg-like domain, confirming evolutionary links with proteins such as VIP36. Protein-carbohydrate and protein-protein interaction studies showed that NdLTL1 binds to both carbohydrates like N-acetylglucosamine, peptidoglycan, lipopolysaccharides (LPS), and mannose, as well as sorting proteins (COPI/COPII). Gene expression analyses indicated that NdLTL1 exhibits the highest expression levels in cardiac tissues and significant upregulation in gills following exposure to Vibrio parahaemolyticus. Recombinant NdLTL1 expressed in Escherichia coli was shown to bind multiple bacterial strains and exhibit calcium-dependent agglutination properties. Enzyme-linked immunosorbent assay (ELISA) confirmed concentration-dependent carbohydrate binding, particularly rapid for LPS. In vitro experiments suggested that recombinant NdLTL1 may promote bacterial growth under nutrient-limited conditions while potentially triggering immune defenses indirectly.

Maackia amurensis seed lectin (MASL) and soluble human podoplanin (shPDPN) sequence analysis and effects on human oral squamous cell carcinoma (OSCC) cell migration and viability

Maackia amurensis lectins serve as research and botanical agents that bind to sialic residues on proteins. For example, M. amurensis seed lectin (MASL) targets the sialic acid modified podoplanin (PDPN) receptor to suppress arthritic chondrocyte inflammation, and inhibit tumor cell growth and motility. However, M. amurensis lectin nomenclature and composition are not clearly defined. Here, we sought to definitively characterize MASL and its effects on tumor cell behavior. We utilized SDS-PAGE and LC-MS/MS to find that M. amurensis lectins can be divided into two groups. MASL is a member of one group which is composed of subunits that form dimers, evidently mediated by a cysteine residue in the carboxy region of the protein. In contrast to MASL, members of the other group do not dimerize under nonreducing conditions. These data also indicate that MASL is composed of 4 isoforms with an identical amino acid sequence, but unique glycosylation sites. We also produced a novel recombinant soluble human PDPN receptor (shPDPN) with 17 threonine residues glycosylated with sialic acid moieties with potential to act as a ligand trap that inhibits OSCC cell growth and motility. In addition, we report here that MASL targets PDPN with very strong binding kinetics in the nanomolar range. Moreover, we confirm that MASL can inhibit the growth and motility of human oral squamous cell carcinoma (OSCC) cells that express the PDPN receptor. Taken together, these data characterize M. amurensis lectins into two major groups based on their intrinsic properties, clarify the composition of MASL and its subunit isoform sequence and glycosylation sites, define sialic acid modifications on the PDPN receptor and its ability to act as a ligand trap, quantitate MASL binding to PDPN with KD in the nanomolar range, and verify the ability of MASL to serve as a potential anticancer agent.

Molecular Modelling and Structure Analysis of Lectins from Vigna linearis

A study was conducted during the year 2022–2023 for in silico analysis of two Vigna linearis lectins in the computer lab, CDFT, Jodhpur, Rajasthan, India. Amino acid sequences of both lectins were obtained from NCBI database and analyzed using different computational tools. Primary structure analysis using ProtParam server revealed acidic, stable and hydrophobic nature of both VLL proteins. Both proteins were predicted heavily glycosylated with a single signal peptide cleavage site (A26-A27). High sequence similarity of both VLL proteins was observed with adzuki, rice bean and moth bean lectins. Both VLL proteins had high proportions of β-sheets in their secondary structure. Good quality 3D structures for both VLL proteins were modelled using Modeller software. A Jelly roll fold, also known as β-sandwich structure was identified in the 3D structure of both VLL proteins. Profunc server annotated both lectins as a carbohydrate binding regulatory protein with significant role in plant defense (GO terms: 0065007, 0006952, 0050896, 0006950, 0009607, 0030246). Galaxy Site web server predicted galactose, A2G (2-acetamido-2-deoxy-α-D-galactopyranose), MFU (Methyl α-L-fucopyranoside) and adenine as common binding ligands for both VLL proteins. Lig Plot analysis revealed hydrogen bonding and hydrophobic interactions were the major bonding interactions between VLL proteins and putative ligands. The results of the study would provide a base for conducting future research on Vigna linearis lectins for different applications.

Genome-wide screening of lectin putative genes from Sorghum bicolor L., distribution in QTLs and a probable implications of lectins in abiotic stress tolerance

BackgroundSorghum bicolor is one of the most important crops worldwide with the potential to provide resilience when other economic staples might fail against the continuous environmental changes. Many physiological, developmental and tolerance traits in plants are either controlled or influenced by lectins; carbohydrate binding proteins. Hence, we aimed at providing a comprehensive in silico account on sorghum’s lectins and study their possible implication on various desired agronomical traits.ResultsWe have searched sorghum’s genome from grain and sweet types for lectins putative genes that encode proteins with domains capable of differentially binding carbohydrate moieties and trigger various physiological responses. Of the 12 known plant lectin families, 8 were identified regarding their domain architectures, evolutionary relationships, physiochemical characteristics, and gene expansion mechanisms, and they were thoroughly addressed. Variations between grain and sweet sorghum lectin homologs in term of the presence/absence of certain other joint domains like dirigent and nucleotide-binding adaptor shared by APAF-1, R-proteins, and CED-4 (NB-ARC) indicate a possible neofunctionalization. Lectin sequences were found to be preferentially overrepresented in certain quantitative trait loci (QTLs) related to various traits under several subcategories such as cold, drought, salinity, panicle/grain composition, and leaf morphology. The co-localization and distribution of lectins among multiple QTLs provide insights into the pleiotropic effects that could be played by one lectin gene in numerous traits.ConclusionOur study offers a first-time inclusive details on sorghum lectins and their possible role in conferring tolerance against abiotic stresses and other economically important traits that can be informative for future functional analysis and breeding studies.

Purification and structural characterization of lectin with antibacterial and anticancer properties from grubs of hide beetle, Dermestes frischii

Lectins or haemagglutinins are diverse classes of non-immune proteins; they bind to carbohydrates and are abundant in nature. In the present study, a coleopteran lectin from grubs of hide beetle, Dermestes frischii called DFL, was purified by glutaraldehyde (fixative-agent) fixed hen erythrocytes and characterized further for its functional properties. The purified DFL was stable between pH range 5 to 9 and heat-stable up to 50 °C. It was insensitive to EDTA and did not require any divalent cations. DFL native molecular mass was approximately 69 kDa with three different polypeptide subunits of 33 (pI ~4.4), 22 (pI ~6) and 14 (pI ~4.4) kDa. Haemagglutinating activity of DFL was highly inhibited by N-acetyl-D-glucosamine. DFL partial peptide sequences obtained from peptide mass fingerprinting experiments matched with amino acid sequences of lectins from different organisms confirmed its nature. Biological properties of purified DFL namely antibacterial and bacterial agglutination experiments revealed that DFL have both the effects against laboratory cultures of Aeromonas hydrophila, Enterococcus faecalis, Escherichia coli and habitat bacterial isolates of Staphylococcus cohnii and Bacillus cereus. In addition, the DFL exhibited substantial anticancer properties against HeLa cells. These results concluded that purified DFL could serve as a potent therapeutic agent for various biomedical applications.

The Jacalin-Related Lectin HvHorcH Is Involved in the Physiological Response of Barley Roots to Salt Stress.

Salt stress tolerance of crop plants is a trait with increasing value for future food production. In an attempt to identify proteins that participate in the salt stress response of barley, we have used a cDNA library from salt-stressed seedling roots of the relatively salt-stress-tolerant cv. Morex for the transfection of a salt-stress-sensitive yeast strain (Saccharomyces cerevisiae YSH818 Δhog1 mutant). From the retrieved cDNA sequences conferring salt tolerance to the yeast mutant, eleven contained the coding sequence of a jacalin-related lectin (JRL) that shows homology to the previously identified JRL horcolin from barley coleoptiles that we therefore named the gene HvHorcH. The detection of HvHorcH protein in root extracellular fluid suggests a secretion under stress conditions. Furthermore, HvHorcH exhibited specificity towards mannose. Protein abundance of HvHorcH in roots of salt-sensitive or salt-tolerant barley cultivars were not trait-specific to salinity treatment, but protein levels increased in response to the treatment, particularly in the root tip. Expression of HvHorcH in Arabidopsis thaliana root tips increased salt tolerance. Hence, we conclude that this protein is involved in the adaptation of plants to salinity.

A Comprehensive Phylogenetic and Bioinformatics Survey of Lectins in the Fungal Kingdom.

Fungal lectins are a large family of carbohydrate-binding proteins with no enzymatic activity. They play fundamental biological roles in the interactions of fungi with their environment and are found in many different species across the fungal kingdom. In particular, their contribution to defense against feeders has been emphasized, and when secreted, lectins may be involved in the recognition of bacteria, fungal competitors and specific host plants. Carbohydrate specificities and quaternary structures vary widely, but evidence for an evolutionary relationship within the different classes of fungal lectins is supported by a high degree of amino acid sequence identity. The UniLectin3D database contains 194 fungal lectin 3D structures, of which 129 are characterized with a carbohydrate ligand. Using the UniLectin3D lectin classification system, 109 lectin sequence motifs were defined to screen 1223 species deposited in the genomic portal MycoCosm of the Joint Genome Institute. The resulting 33,485 putative lectin sequences are organized in MycoLec, a publicly available and searchable database. These results shed light on the evolution of the lectin gene families in fungi.

Mucoricin is a ricin-like toxin that is critical for the pathogenesis of mucormycosis.

Fungi of the order Mucorales cause mucormycosis, a lethal infection with an incompletely understood pathogenesis. We now demonstrate that Mucorales fungi produce a toxin that plays a central role in virulence. Polyclonal antibodies against this toxin inhibit its ability to damage human cells in vitro, and prevent hypovolemic shock, organ necrosis, and death in mice with mucormycosis. RNAi inhibition of the toxin in Rhizopus delemar, compromises the ability of the fungus to damage host cells and attenuates virulence in mice. This 17 kDa toxin has structural and functional features of the plant toxin, ricin, including the ability to inhibit protein synthesis by its N-glycosylase activity, the existence of a motif that mediates vascular leak, and a lectin sequence. Antibodies against the toxin inhibit R. delemar- or toxin-mediated vascular permeability in vitro and cross-react with ricin. A monoclonal anti-ricin B chain antibody binds to the toxin and also inhibits its ability to cause vascular permeability. Therefore, we propose the name “mucoricin” for this toxin. Not only is mucoricin important in the pathogenesis of mucormycosis but our data suggest that a ricin-like toxin is produced by organisms beyond the plant and bacterial kingdoms. Importantly, mucoricin should be a promising therapeutic target.

Transcriptome- based analysis of the diversity of membrane-bound lectins in Baikal amphipods Eulimnogammarus sp. and the Holarctic amphipod Gammarus lacustris

The aim of this study was transcriptome-based analysis of the diversity of membrane-bound lectins in Baikal amphipods Eulimnogammarus verrucosus and E. cyaneus and a Holarctic amphipod Gammarus lacustris. The results of this study show that studied species of amphipods possess quite similar repertoires of lectins. The obtained lectin sequence data can be used in further molecular-level exploration of amphipod physiology.

Purification and Biochemical Characterization of Selected F-Type Lectins.

The purification of fucose-binding lectins from the liver of striped bass (Morone saxatilis), a teleost fish, and the identification of a novel lectin sequence motif led to the identification of a new family of lectins, the F-type lectins (FTLs) (see overview of the FTL family in Chapter 23 ). Isolation and purification of these proteins from liver extracts of striped bass was accomplished by affinity chromatography and size exclusion, and their identification as FTLs, by direct Edman sequencing, and protein, transcript, and gene sequence analysis. The development of specific antibodies against the M. saxatilis FTL provided an additional tool for the identification of FTLs. These methods have been successfully used for the purification of the FTL family members from tissues and body fluids of various animal species. Production and characterization of FTLs has been facilitated by the expression of the recombinant proteins. In this chapter, the biochemical characterization of FTLs is focused on the analysis of their carbohydrate specificity.

Messages From the Past: New Insights in Plant Lectin Evolution.

Lectins are a large and diverse class of proteins, found in all kingdoms of life. Plants are known to express different types of carbohydrate-binding proteins, each containing at least one particular lectin domain which enables them to specifically recognize and bind carbohydrate structures. The group of plant lectins is heterogeneous in terms of structure, biological activity and function. Lectins control various aspects of plant development and defense. Some lectins facilitate recognition of exogenous danger signals or play a role in endogenous signaling pathways, while others are considered as storage proteins or involved in symbiotic relationships. In this study, we revisit the origin of the different plant lectin families in view of the recently reshaped tree of life. Due to new genomic sampling of previously unknown microbial lineages, the tree of life has expanded and was reshaped multiple times. In addition, more plant genomes especially from basal Phragmoplastophyta, bryophytes, and Salviniales (e.g., Chara braunii, Marchantia polymorpha, Physcomitrella patens, Azolla filiculoides, and Salvinia cucullata) have been analyzed, and annotated genome sequences have become accessible. We searched 38 plant genome sequences including core eudicots, monocots, gymnosperms, fern, lycophytes, bryophytes, charophytes, chlorophytes, glaucophytes, and rhodophytes for lectin motifs, performed an extensive comparative analysis of lectin domain architectures, and determined the phylogenetic and evolutionary history of lectins in the plant lineage. In conclusion, we describe the conservation of particular domains in plant lectin sequences obtained from algae to higher plants. The strong conservation of several lectin motifs highlights their significance for plants.

Effect of naturally occurring variations of the F-type lectin sequence motif on glycan binding: studies on F-type lectin domains with typical and atypical sequence motifs.

The typical F-type lectin domain (FLD) has an L-fucose-binding motif [HX(26)RXDX(4)R/K] with conserved basic residues that mediate hydrogen bonding with alpha-L-fucose. About one-third of the nonredundant FLD sequences in the publicly available databases are "atypical"; they have motifs with substitutions of these critical residues and/or variations in motif length. We addressed the question if atypical FLDs with substitutions of the critical residues retain lectin activity by performing site-directed mutagenesis and assessing the glycan-binding functions of typical and atypical FLDs. Site directed mutagenesis of an L-fucose-binding FLD from Streptosporangium roseum indicated that the critical His residue could be replaced by Ser and the second Arg by Lys without complete loss of lectin activity. Mutagenesis of His to other naturally substituting residues and mutagenesis of the first Arg to the naturally substituting residues, Lys, Ile, Ser, or Cys, resulted in loss of lectin activity. Glycan binding analysis and site-directed mutagenesis of atypical FLDs from Actinomyces turicensis, and Saccharomonospora cyanea confirmed that Ser and Thr can assume the L-fucose-binding role of the critical His, and further suggested that the residue in this position is dispensable in certain FLDs. We identified, by sequence and structural analysis of atypical FLDs, a Glu residue in the complementarity determining region, CDR5 that compensates for a lack of the critical His or other appropriate polar residue in this position. We propose that FLDs lacking a typical FLD sequence motif might nevertheless retain lectin activity through the recruitment of other strategically positioned polar residues in the CDR loops. © 2018 IUBMB Life, 71(3):385-397, 2019.

Deciphering Protein Glycosylation by Computational Integration of On-chip Profiling, Glycan-array Data, and Mass Spectrometry.

The difficulty in uncovering detailed information about protein glycosylation stems from the complexity of glycans and the large amount of material needed for the experiments. Here we report a method that gives information on the isomeric variants of glycans in a format compatible with analyzing low-abundance proteins. On-chip glycan modification and probing (on-chip gmap) uses sequential and parallel rounds of exoglycosidase cleavage and lectin profiling of microspots of proteins, together with algorithms that incorporate glycan-array analyses and information from mass spectrometry, when available, to computationally interpret the data. In tests on control proteins with simple or complex glycosylation, on-chip gmap accurately characterized the relative proportions of core types and terminal features of glycans. Subterminal features (monosaccharides and linkages under a terminal monosaccharide) were accurately probed using a rationally designed sequence of lectin and exoglycosidase incubations. The integration of mass information further improved accuracy in each case. An alternative use of on-chip gmap was to complement the mass spectrometry analysis of detached glycans by specifying the isomers that comprise the glycans identified by mass spectrometry. On-chip gmap provides the potential for detailed studies of glycosylation in a format compatible with clinical specimens or other low-abundance sources.

Nature-inspired engineering of an F-type lectin for increased binding strength.

Individual lectin-carbohydrate interactions are usually of low affinity. However, high avidity is frequently attained by the multivalent presentation of glycans on biological surfaces coupled with the occurrence of high order lectin oligomers or tandem repeats of lectin domains in the polypeptide. F-type lectins are l-fucose binding lectins with a typical sequence motif, HX(26)RXDX(4)R/K, whose residues participate in l-fucose binding. We previously reported the presence of a few eukaryotic F-type lectin domains with partial sequence duplication that results in the presence of two l-fucose-binding sequence motifs. We hypothesized that such partial sequence duplication would result in greater avidity of lectin-ligand interactions. Inspired by this example from Nature, we attempted to engineer a bacterial F-type lectin domain from Streptosporangium roseum to attain avid binding by mimicking partial duplication. The engineered lectin demonstrated 12-fold greater binding strength than the wild-type lectin to multivalent fucosylated glycoconjugates. However, the affinity to the monosaccharide l-fucose in solution was similar and partial sequence duplication did not result in an additional functional l-fucose binding site. We also cloned, expressed and purified a Branchiostoma floridae F-type lectin domain with naturally occurring partial sequence duplication and confirmed that the duplicated region with the F-type lectin sequence motif did not participate in l-fucose binding. We found that the greater binding strength of the engineered lectin from S. roseum was instead due to increased oligomerization. We believe that this Nature-inspired strategy might be useful for engineering lectins to improve binding strength in various applications.

Signaling through plant lectins: modulation of plant immunity and beyond.

Lectins constitute an abundant group of proteins that are present throughout the plant kingdom. Only recently, genome-wide screenings have unraveled the multitude of different lectin sequences within one plant species. It appears that plants employ a plurality of lectins, though relatively few lectins have already been studied and functionally characterized. Therefore, it is very likely that the full potential of lectin genes in plants is underrated. This review summarizes the knowledge of plasma membrane-bound lectins in different biological processes (such as recognition of pathogen-derived molecules and symbiosis) and illustrates the significance of soluble intracellular lectins and how they can contribute to plant signaling. Altogether, the family of plant lectins is highly complex with an enormous diversity in biochemical properties and activities.

Genome-Wide Screening for Lectin Motifs in Arabidopsis thaliana.

For more than three decades, served as a model for plant biology research. At present only a few protein families have been studied in detail in . This study focused on all sequences with lectin motifs in the genome of . Based on amino acid sequence similarity (BLASTp searches), 217 putative lectin genes were retrieved belonging to 9 out of 12 different lectin families. The domain organization and genomic distribution for each lectin family were analyzed. Domain architecture analysis revealed that most of these lectin gene sequences are linked to other domains, often belonging to protein families with catalytic activity. Many protein domains identified are known to play a role in stress signaling and defense, suggesting a major contribution of the putative lectins in development and plant defense. This genome-wide screen for different lectin motifs will help to unravel the functional characteristics of lectins. In addition, phylogenetic trees and WebLogos were created and showed that most lectin sequences that share the same domain architecture evolved together. Furthermore, the amino acids responsible for carbohydrate binding are largely conserved. Our results provide information about the evolutionary relationships and functional divergence of the lectin motifs in .

CDNA cloning, molecular modeling and docking calculations of L-type lectins from Swartzia simplex var. grandiflora (Leguminosae, Papilionoideae), a member of the tribe Swartzieae

The genus Swartzia is a member of the tribe Swartzieae, whose genera constitute the living descendants of one of the early branches of the papilionoid legumes. Legume lectins comprise one of the main families of structurally and evolutionarily related carbohydrate-binding proteins of plant origin. However, these proteins have been poorly investigated in Swartzia and to date, only the lectin from S. laevicarpa seeds (SLL) has been purified. Moreover, no sequence information is known from lectins of any member of the tribe Swartzieae. In the present study, partial cDNA sequences encoding L-type lectins were obtained from developing seeds of S. simplex var. grandiflora. The amino acid sequences of the S. simplex grandiflora lectins (SSGLs) were only averagely related to the known primary structures of legume lectins, with sequence identities not greater than 50–52%. The SSGL sequences were more related to amino acid sequences of papilionoid lectins from members of the tribes Sophoreae and Dalbergieae and from the Cladratis and Vataireoid clades, which constitute with other taxa, the first branching lineages of the subfamily Papilionoideae. The three-dimensional structures of 2 representative SSGLs (SSGL-A and SSGL-E) were predicted by homology modeling using templates that exhibit the characteristic β-sandwich fold of the L-type lectins. Molecular docking calculations predicted that SSGL-A is able to interact with D-galactose, N-acetyl-D-galactosamine and α-lactose, whereas SSGL-E is probably a non-functional lectin due to 2 mutations in the carbohydrate-binding site. Using molecular dynamics simulations followed by density functional theory calculations, the binding free energies of the interaction of SSGL-A with GalNAc and α-lactose were estimated as −31.7 and −47.5 kcal/mol, respectively. These findings gave insights about the carbohydrate-binding specificity of SLL, which binds to immobilized lactose but is not retained in a matrix containing D-GalNAc as ligand.

Molecular characterization of snowdrop lectin (GNA) and its comparison with reported lectin sequences of Amaryllidaceae

Plant lectins have become efficient sources of insect resistance in crops. The present study was conducted to identify, amplify, clone and characterize the plant lectin gene GNA. The lectin, present in Galanthus nivalis (snowdrop), is an agglutinin toxic to hemiptera. The attempt was made to elucidate the relationship of the lectin gene trGNA (GNA isolated and characterized from Turkey) with other previously cloned lectins having insecticidal activity and to ensure the presence of the conserved mannose-binding region/site in the gene sequence. The full-length cDNA of trGNA was 477 bp that contained a 333 bp open reading frame encoding 157 amino acid proteins with 23 amino acids of signal peptide. BLAST results showed that trGNA has 89-97% similarity with previously reported GNA sequences while it has 84-96% similarity with earlier reported GNA protein sequences. No intron was detected within the region of genomic sequence corresponding to trGNA full-length cDNA. According to the search results from the NCBI (National Centrer for Biotechnology Information database), trGNA from Galanthus nivalis is most similar to the previously reported lectin sequences of Narcissus tazetta with a similarity percentage of 87%. The obtained results are useful for engineering of plants with enhanced insecticidal activity against chewing and sucking insects, causing crop pests. In addition, medical application of lectins may also be considered.

Genome-wide identification and domain organization of lectin domains in cucumber

Lectins are ubiquitous proteins in plants and play important roles in a diverse set of biological processes, such as plant defense and cell signaling. Despite the availability of the Cucumis sativus L. genome sequence since 2009, little is known with respect to the occurrence of lectins in cucumber. In this study, a total of 146 putative lectin genes belonging to 10 different lectin families were identified and localized in the cucumber genome. Domain architecture analysis revealed that most of these lectin gene sequences contain multiple domains, where lectin domains are linked with other domains, as such creating chimeric lectin sequences encoding proteins with dual activities. This study provides an overview of lectin motifs in cucumber and will help to understand their potential biological role(s).

Isolation and Characterization of Mannose-Binding Lectin Gene from Leaves of <I>Allium ascalonicum</I> (Shallot) and its Putative Role in Insect Resistance

Plant lectins are the heterogenous group of glycoproteins extensively studied for their potent insecticidal property against Hemipteran pests. In this present study, the full‐length cDNA of monocot mannose‐binding insecticidal lectin gene was isolated from Allium ascalonicum leaves. The isolated Allium ascalonicum Lectin (AAL) gene was cloned in pGEM‐T vector, sequenced and the sequence was submitted to GenBank (KM096570.1). Sequence analysis revealed a 468 bp open reading frame (ORF) encoding a putative 155 amino acids agglutinin precursor. Multiple sequence alignment and phylogenetic analysis of AAL amino acid with those of 30 other Mannose binding lectin (MBL) sequences in NCBI revealed a high similarity of 85‐95% indicating that AAL is a member of the MBL super family and forms a cluster with other onion lectins. Secondary structure prediction and the homology modeling showed that AAL protein possess predominantly β‐sheets and three potential mannose‐binding motifs consisting of 5 amino acid residues QDNVY like other GNA lectins. The results of the insilico analysis predict that the Allium ascalonicum lectin gene can be another potent insecticidal protein.