Molecular and functional characterization of a glycosylated Galactose-Binding lectin from Mytilus californianus

Garcia-Maldonado, E.; Cano‐Sánchez, Patricia; Hernández-Santoyo, Alejandra

doi:10.1016/j.fsi.2017.05.057

Cited by 30 publications

(25 citation statements)

References 38 publications

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“…Probably, these differences between the structures obtained by each purification process were due to the recognition of the complex of different molecules. Thus, whereas the stroma column has several sugar sequences, the galactose column has only one, that could facilitate the purification of a tetrameric complex by the oligomerization, induced by recognition of the same sugar, as previously reported for the lectin purified from Mytilus californianus [49]. Also, the use of acetic acid in a stroma column to dialysis the protein did not allow a reversion to the same quaternary structure that was previously eluted.…”

Section: Discussionmentioning

confidence: 82%

The B Subunit of PirABvp Toxin Secreted from Vibrio parahaemolyticus Causing AHPND Is an Amino Sugar Specific Lectin

et al. 2020

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Vibrio parahaemolyticus (Vp) is the etiological agent of the acute hepatopancreatic necrosis disease (AHPND) in Penaeus vannamei shrimp. Vp possesses a 63–70 kb conjugative plasmid that encodes the binary toxin PirAvp/PirBvp. The 250 kDa PirABvp complex was purified by affinity chromatography with galactose-sepharose 4B and on a stroma from glutaraldehyde-fixed rat erythrocytes column, as a heterotetramer of PirAvp and PirBvp subunits. In addition, recombinant pirB (rPirBvp) and pirA (rPirAvp) were obtained. The homogeneity of the purified protein was determined by SDS-PAGE analysis, and the yield of protein was 488 ng/100 μg of total protein of extracellular products. The PirABvp complex and the rPirBvp showed hemagglutinating activity toward rat erythrocytes. The rPirAvp showed no hemagglutinating capacity toward the animal red cells tested. Among different mono and disaccharides tested, only GalNH2 and GlcNH2 were able to inhibit hemagglutination of the PirABvp complex and the rPirBvp. Glycoproteins showed inhibitory specificity, and fetuin was the glycoprotein that showed the highest inhibition. Other glycoproteins, such as mucin, and glycosaminoglycans, such as heparin, also inhibited the activity. Desialylation of erythrocytes enhanced the hemagglutinating activity. This confirms that Gal or Gal (β1,4) GlcNAc are the main ligands for PirABvp. The agglutinating activity of the PirABvp complex and the rPirBvp is not dependent on cations, because addition of Mg2+ or Ca2+ showed no effect on the protein capacity. Our results strongly suggest that the PirBvp subunit is a lectin, which is part of the PirA/PirBvp complex, and it seems to participate in bacterial pathogenicity.

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Section: Discussionmentioning

confidence: 82%

The B Subunit of PirABvp Toxin Secreted from Vibrio parahaemolyticus Causing AHPND Is an Amino Sugar Specific Lectin

et al. 2020

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“…MCL has specificity for d ‐galactose and N ‐acetyl‐ d ‐galactosamine; this lectin was able to agglutinate and inhibit the growth of Lactobacillus plantarum and E. coli (García‐Maldonado et al . ).…”

Section: Molecular Characteristics Of Antimicrobial Lectinsmentioning

confidence: 97%

Lectins as antimicrobial agents

et al. 2018

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Summary The resistance of micro‐organisms to antimicrobial agents has been a challenge to treat animal and human infections, and for environmental control. Lectins are natural proteins and some are potent antimicrobials through binding to carbohydrates on microbial surfaces. Oligomerization state of lectins can influence their biological activity and maximum binding capacity; the association among lectin polypeptide chains can alter the carbohydrate–lectin binding dissociation rate constants. Antimicrobial mechanisms of lectins include the pore formation ability, followed by changes in the cell permeability and latter, indicates interactions with the bacterial cell wall components. In addition, the antifungal activity of lectins is associated with the chitin‐binding property, resulting in the disintegration of the cell wall or the arrest of de novo synthesis from the cell wall during fungal development or division. Quorum sensing is a cell‐to‐cell communication process that allows interspecies and interkingdom signalling which coordinate virulence genes; antiquorum‐sensing therapies are described for animal and plant lectins. This review article, among other approaches, evaluates lectins as antimicrobials.

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“…Since no R‐type lectin had been biochemically purified from the family Mytilidae, mytilectins were considered for some time to be the only β‐trefoil lectins present in mytilids, and it was speculated that their natural function related to the innate immune response . However, the isolation of a novel lectin from the purplish bifurcate mussel ( Mytilisepta virgata ) in this study suggests the possibility of greater diversification among lectins in this family.…”

Section: Introductionmentioning

confidence: 82%

A GM1b/asialo‐GM1 oligosaccharide‐binding R‐type lectin from purplish bifurcate mussels Mytilisepta virgata and its effect on MAP kinases

et al. 2019

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A 15‐kDa lectin, termed SeviL, was isolated from Mytilisepta virgata (purplish bifurcate mussel). SeviL forms a noncovalent dimer that binds strongly to ganglio‐series GM1b oligosaccharide (Neu5Acɑ2‐3Galβ1‐3GalNAcβ1‐4Galβ1‐4Glc) and its precursor, asialo‐GM1 (Galβ1‐3GalNAcβ1‐4Galβ1‐4Glc). SeviL also interacts weakly with the glycan moiety of SSEA‐4 hexaose (Neu5Acα2‐3Galβ1‐3GalNAcβ1‐3Galα1‐4Galβ1‐4Glc). A partial protein sequence of the lectin was determined by mass spectrometry, and the complete sequence was identified from transcriptomic analysis. SeviL, consisting of 129 amino acids, was classified as an R(icin B)‐type lectin, based on the presence of the QxW motif characteristic of this fold. SeviL mRNA is highly expressed in gills and, in particular, mantle rim tissues. Orthologue sequences were identified in other species of the family Mytilidae, including Mytilus galloprovincialis, from which lectin MytiLec‐1 was isolated and characterized in our previous studies. Thus, mytilid species contain lectins belonging to at least two distinct families (R‐type lectins and mytilectins) that have a common β‐trefoil fold structure but differing glycan‐binding specificities. SeviL displayed notable cytotoxic (apoptotic) effects against various cultured cell lines (human breast, ovarian, and colonic cancer; dog kidney) that possess asialo‐GM1 oligosaccharide at the cell surface. This cytotoxic effect was inhibited by the presence of anti‐asialo‐GM1 oligosaccharide antibodies. With HeLa ovarian cancer cells, SeviL showed dose‐ and time‐dependent activation of kinase MKK3/6, p38 MAPK, and caspase‐3/9. The transduction pathways activated by SeviL via the glycosphingolipid oligosaccharide were triggered apoptosis. Database Nucleotide sequence data have been deposited in the GenBank database under accession numbers , , , , , , , , , , and .

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Molecular and functional characterization of a glycosylated Galactose-Binding lectin from Mytilus californianus

Cited by 30 publications

References 38 publications

The B Subunit of PirABvp Toxin Secreted from Vibrio parahaemolyticus Causing AHPND Is an Amino Sugar Specific Lectin

The B Subunit of PirABvp Toxin Secreted from Vibrio parahaemolyticus Causing AHPND Is an Amino Sugar Specific Lectin

Lectins as antimicrobial agents

A GM1b/asialo‐GM1 oligosaccharide‐binding R‐type lectin from purplish bifurcate mussels Mytilisepta virgata and its effect on MAP kinases

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