A review on the antimicrobial properties of lectins

Fonseca, Victor Juno Alencar; Braga, Ana Lays; Ribeiro-Filho, Jaime; Teixeira, Claudener S.; Hora, Gabriel C. A. da; Morais-Braga, Maria Flaviana Bezerra

doi:10.1016/j.ijbiomac.2021.11.209

Cited by 39 publications

(12 citation statements)

References 80 publications

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“…Plant lectin proteins exhibit thermophilic and hydrophobic properties and play a role in antimicrobial activity. The lectins adhere to carbohydrates on the pathogen’s surface, which can degrade the cell wall and inhibit microbes from binding to host cells ( Roberts and Goldstein, 1982 ; Pusztai and Grant, 1998 ; Fonseca et al., 2022 ). Similarly, crambin is another hydrophobic plant protein that belongs to the thionin family ( Teeter et al., 1981 ; García Olmedo et al., 1989 ).…”

Section: Resultsmentioning

confidence: 99%

In silico characterization of differentially expressed short-read nucleotide sequences identified in dieback stress-induced transcriptomic analysis reveals their role as antimicrobial peptides

Ijaz

Haq²,

Malik³

et al. 2023

Front. Plant Sci.

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We investigated the in silico characterization of short-length nucleotide sequences that were differentially expressed in dieback stress-induced transcriptomic analysis. They displayed homology with C-terminal flanking peptides and defensins-like proteins, revealing their antimicrobial activity. Their predicted fingerprints displayed protein signatures related to antimicrobial peptides. These short-length RGAs have been shown to possess structural motifs such as APLT P-type ATPase, casein kinase II (CK2), protein kinase 3, protein kinase C (PKC), and N-glycosylation site that are the attributes of disease resistance genes. The prediction of arginine and lysine residues in active binding sites in ligand docking analysis prophesied them as antimicrobial peptides due to their strong relation with antimicrobial activity. The in silico structural–functional characterization has predicted their role in resistance against microbial pathogens. Moreover, the predicted antimicrobial peptide regions showed their homology with the signature domain of PR-5-like protein and AMP family Thaumatin

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Section: Resultsmentioning

confidence: 99%

In silico characterization of differentially expressed short-read nucleotide sequences identified in dieback stress-induced transcriptomic analysis reveals their role as antimicrobial peptides

Ijaz

Haq²,

Malik³

et al. 2023

Front. Plant Sci.

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“…In research carried out by Fonseca et al ( 2022 ), lectins of natural origin are pointed out for having remarkable antimicrobial activity. Due to their ability to selectively bind to carbohydrates, they can interact in various ways on the cell wall of bacteria, fungi and protozoa.…”

Section: Discussionmentioning

confidence: 99%

Lectins ConA and ConM extracted from Canavalia ensiformis (L.) DC and Canavalia rosea (Sw.) DC inhibit planktonic Candida albicans and Candida tropicalis

et al. 2022

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“…The role of BnLegLus in Leg-T remains unclear, as the function of their homologs in A. thaliana is unknown (Figure 2). The BnLegLu genes containing the kinase domain in cluster III may respond to S. sclerotiorum through stress signal transduction (Bellande et al, 2017); while the four BnLegLus genes in cluster VI whose expression was induced by SD may recognize and respond to S. sclerotiorum hyphae as a function of classical lectins (De Coninck and Van Damme, 2021;Fonseca et al, 2022; Figure 2). Previous studies have shown that lectins can bind to hyphae, resulting in the swelling of hyphae, vacuolation of the cell content, destruction of the nutrient absorption of the fungi, interference with spore germination, and even cell wall lysis (Lagarda-Diaz et al, 2017;Katoch and Tripathi, 2021).…”

Section: Discussionmentioning

confidence: 99%

“…Mechanically, the antifungal activity of legume lectins can be mainly ascribed to the indirect effect of their binding with cell wall components, which can affect fungal survival or other activities like spore germination (Leal et al, 2012). Some legume seed proteins can bind with carbohydrate components of the bacterial cell wall or extracellular glycans and prevent the entry of microorganisms into the cytoplasm (Fonseca et al, 2022). Previous studies have demonstrated that lectins from chickpea have antibacterial activity against some bacterial pathogens such as Escherichia coli, Bacillus subtilis, Salmonella marcescens, and Pseudomonas syringae (Gautam et al, 2018a).…”

Section: Introductionmentioning

confidence: 99%

Genome-wide identification and functional exploration of the legume lectin genes in Brassica napus and their roles in Sclerotinia disease resistance

Zuo

Xie²,

Gao³

et al. 2022

Front. Plant Sci.

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As one of the largest classes of lectins, legume lectins have a variety of desirable features such as antibacterial and insecticidal activities as well as anti-abiotic stress ability. The Sclerotinia disease (SD) caused by the soil-borne fungus Sclerotinia sclerotiorum is a devastating disease affecting most oil crops such as Brassica napus. Here, we identified 130 legume lectin (LegLu) genes in B. napus, which could be phylogenetically classified into seven clusters. The BnLegLu gene family has been significantly expanded since the whole-genome duplication (WGD) or segmental duplication. Gene structure and conserved motif analysis suggested that the BnLegLu genes were well conserved in each cluster. Moreover, relative to those genes only containing the legume lectin domain in cluster VI–VII, the genes in cluster I–V harbored a transmembrane domain and a kinase domain linked to the legume lectin domain in the C terminus. The expression of most BnLegLu genes was relatively low in various tissues. Thirty-five BnLegLu genes were responsive to abiotic stress, and 40 BnLegLu genes were strongly induced by S. sclerotiorum, with a most significant up-regulation of 715-fold, indicating their functional roles in SD resistance. Four BnLegLu genes were located in the candidate regions of genome-wide association analysis (GWAS) results which resulted from a worldwide rapeseed population consisting of 324 accessions associated with SD. Among them, the positive role of BnLegLus-16 in SD resistance was validated by transient expression in tobacco leaves. This study provides important information on BnLegLu genes, particularly about their roles in SD resistance, which may help targeted functional research and genetic improvement in the breeding of B. napus.

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A review on the antimicrobial properties of lectins

Cited by 39 publications

References 80 publications

In silico characterization of differentially expressed short-read nucleotide sequences identified in dieback stress-induced transcriptomic analysis reveals their role as antimicrobial peptides

In silico characterization of differentially expressed short-read nucleotide sequences identified in dieback stress-induced transcriptomic analysis reveals their role as antimicrobial peptides

Lectins ConA and ConM extracted from Canavalia ensiformis (L.) DC and Canavalia rosea (Sw.) DC inhibit planktonic Candida albicans and Candida tropicalis

Genome-wide identification and functional exploration of the legume lectin genes in Brassica napus and their roles in Sclerotinia disease resistance

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