Structure and engineering of tandem repeat lectins

Notova, Simona; Bonnardel, François; Lisacek, Frédérique; Varrot, A.; Imberty, Anne

doi:10.1016/j.sbi.2019.11.006

Cited by 34 publications

(33 citation statements)

References 55 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For instance, β-trefoil lectins are widespread and have been reported in bacteria, fungi, plants and animals. These lectin domains are often attached to other protein domains with toxic or enzymatic activity [35,159].…”

Section: Similarities and Differences Between Plant Lectins And Lectimentioning

confidence: 99%

130 years of Plant Lectin Research

2020

View full text Add to dashboard Cite

Lectins are proteins with diverse molecular structures that share the ability to recognize and bind specifically and reversibly to carbohydrate structures without changing the carbohydrate moiety. The history of lectins started with the discovery of ricin about 130 years ago but since then our understanding of lectins has dramatically changed. Over the years the research focus was shifted from 'the characterization of carbohydrate-binding proteins' to 'understanding the biological function of lectins'. Nowadays plant lectins attract a lot of attention especially because of their potential for crop improvement and biomedical research, as well as their application as tools in glycobiology. The present review aims to give an overview of plant lectins and their applications, and how the field evolved in the last decades.

show abstract

Section: Similarities and Differences Between Plant Lectins And Lectimentioning

confidence: 99%

130 years of Plant Lectin Research

2020

View full text Add to dashboard Cite

show abstract

“…This finding means that all of these plant lectins are chimerolectins by structure [ 50 ]. The organization of LdRBLk also differs from the domain architecture in bacteria and fungi, in which the pfam00652 domain is usually repeated two or three times [ 52 ].…”

Section: Discussionmentioning

confidence: 99%

Identification of the Ricin-B-Lectin LdRBLk in the Colorado Potato Beetle and an Analysis of Its Expression in Response to Fungal Infections

Rotskaya¹,

Kryukov²,

Kosman³

et al. 2021

JoF

View full text Add to dashboard Cite

Ricin-B-lectins (RBLs) have been identified in many groups of organisms, including coleopterans insects, particularly the Colorado potato beetle Leptinotarsa decemlineata (LdRBLs). We hypothesized that one of these LdRBLs (LdRBLk) may be involved in the immune response to fungal infections. We performed a theoretical analysis of the structure of this protein. Additionally, the expression levels of the LdRBlk gene were measured in L. decemlineata in response to infections with the fungi Metarhizium robertsii and Beauveria bassiana. The expression levels of LdRBlk in the L. decemlineata cuticle and fat body were increased in response to both infections. The induction of LdRBlk expression was dependent on the susceptibility of larvae to the fungi. Upregulation of the LdRBlk gene was also observed in response to other stresses, particularly thermal burns. Elevation of LdRBlk expression was frequently observed to be correlated with the expression of the antimicrobial peptide attacin but was not correlated with hsp90 regulation. Commercially available β-lectin of ricin from Ricinus communis was observed to inhibit the germination of conidia of the fungi. We suggest that LdRBLk is involved in antifungal immune responses in the Colorado potato beetle, either exerting fungicidal properties directly or acting as a modulator of the immune response.

show abstract

“…The most represented classes include galectin-like (18%), PA14 yeast adhesin (15%), AAL-like (12%), fungal fruit body lectin (11%) and Boletus and Laetiporus ß-trefoil lectin (7%) (Figure 1). While lectins are often forming multivalent protein complexes through monomer oligomerization, several fungal lectins generate multivalent binding sites through internal repeats, as in the case of ß-trefoils and ß-propellers [34].…”

Section: Structural Classification Of Fungal Lectins In Unilectin3dmentioning

confidence: 99%

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

Lebreton

Bonnardel

Dai

et al. 2021

JoF

Self Cite

View full text Add to dashboard Cite

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.

show abstract

Structure and engineering of tandem repeat lectins

Cited by 34 publications

References 55 publications

130 years of Plant Lectin Research

130 years of Plant Lectin Research

Identification of the Ricin-B-Lectin LdRBLk in the Colorado Potato Beetle and an Analysis of Its Expression in Response to Fungal Infections

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

Contact Info

Product

Resources

About