Purification and characterization of a highly thermostable GlcNAc-binding lectin from Collaea speciosa seeds

Oliveira, M. R. de; Osterne, Vinicius Jose Da Silva; Lossio, Claudia Figueiredo; Serna, Sonia; Reichardt, Niels; Nascimento, Kyria S.; Damme, Els J. M. Van; Cavada, Benildo Sousa

doi:10.1016/j.ijbiomac.2021.10.219

Cited by 4 publications

(3 citation statements)

References 61 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The lectin proved to be thermostable with maximum activity at temperatures of 30 ºC, 40 ºC and 50 ºC, but its activity was reduced when 100 ºC was reached. Other lectins of the same botanical family show maximum activity at similar temperatures, such as the Collaea speciosa lectin isolated by Oliveira et al (2021) and the lectin isolated by Alves et al (2015) from seeds of Clathrotropis nitida, which showed low hemagglutinating activity at 100 ºC. Total dependence of CiL on divalent ions, as noted above, closely resembled the findings of Pinto-Junior et al (2016) who isolated a metal-dependent lectin from the seeds of Dioclea reflexa.…”

Section: Physicochemical Characterizationsupporting

confidence: 71%

A new lectin from Crotalaria incana seeds and studies of toxicity in Artemia salina nauplii

Pereira,

Martins,

Oliveira

et al. 2024

Acta Bot. Bras.

View full text Add to dashboard Cite

Lectins are proteins that recognize and bind to carbohydrates in a reversible and specific manner. In this work, a lectin from Crotalaria incana L. seeds was purified by Sephadex G-50 affinity chromatography. The purified lectin was named CiL and presented affinity towards D-mannose, D-glucose, D-galactose, α-methyl-D-mannoside and derivatives. CiL was stable over a wide range of temperatures and pH values, and it was divalent cation-dependent. SDS-PAGE analysis indicated that CiL is composed of two subunits with apparent masses of 29 and 30 kDa. The amino acid sequence of five tryptic peptides was obtained through mass spectrometry. Partial primary structure data indicated the similarity between CiL and lectins from Phaseolus vulgaris, Cladrastis kentukea, Lens culinaris, Pisum sativum, Crotalaria pallida and C. juncea. CiL showed no toxicity to Artemia salina nauplii at the concentration of 2 mg/mL, thus reinforcing the potential of this protein for further studies in other biological models and elucidation of possible effects.

show abstract

Section: Physicochemical Characterizationsupporting

confidence: 71%

A new lectin from Crotalaria incana seeds and studies of toxicity in Artemia salina nauplii

Pereira,

Martins,

Oliveira

et al. 2024

Acta Bot. Bras.

View full text Add to dashboard Cite

show abstract

“…Lectins are a class of non-immune proteins or glycoproteins that can specifically and reversibly bind to sugars, and have the functions of agglutinating cells and precipitating polysaccharides or glycoconjugates [1,2]. Recent studies have found that lectins have certain anti-cancer properties, as they can directly inhibit the proliferation of malignant tumor cells without affecting the growth of normal cells [3].…”

Section: Introductionmentioning

confidence: 99%

Research on the Anti-Tumor Mechanism of Artocarpus Lingnanensis Lectin

Li,

Chen,

et al. 2024

J Clin Med Res

View full text Add to dashboard Cite

The purpose of this study was to investigate the mechanism of Artocarpus Lingnanensis Lectin (ALL) in inhibiting the growth of tumor cells EL-4. ALL was applied to mouse lymphoma cells EL-4, with PHA (100μg/mL) as a positive control drug. The toxicity of ALL (3.125, 6.25, 12.5, 25, 50, 100, 200μg/mL) on EL-4 cells was evaluated using the CCK-8 assay. Flow cytometry was used to assess the effect of ALL (25, 100 μg/ mL) on apoptosis and cell membrane potential of EL-4 cells. Western blotting was conducted to measure the protein expression levels of BAX, cleaved-Caspase-3, cleaved-Caspase-9, cleaved-PARP1. Fluorescence microscopy was employed to detect the concentration of free calcium ions. Results showed that compared to the control group, ALL had a significant inhibitory effect on EL-4 cells in a dose-dependent manner, with an IC50 value of 105.4μg/mL. Flow cytometry results indicated an increase in apoptosis rate of EL-4 cells with ALL treatment, leading to a higher proportion of depolarized mitochondrial membrane potential. Furthermore, the protein expression levels of BAX, cleaved-Caspase-3, cleaved-Caspase-9, and cleaved-PARP1 were significantly upregulated. In conclusion, ALL can promote apoptosis of EL-4 cells through the mitochondrial apoptosis pathway, inhibit their migration and invasion, and thereby exhibit anti-tumor effects.

show abstract

“…Such proteins include, for example, the water-soluble, plasmalemma-bound potato lectin, GlcNAc-specific lectin II from Griffonia simplicifolia, as well as wheat germ agglutinin (WGA) etc. De novo WGA synthesis in meristematic tissues of roots and above-ground part of seedlings of wheat has been established [5][6][7]. It is known that plant lectins and proteins with one or more lectin domains represent a major part of some membrane-bound and soluble pattern recognition receptors (PRRs).…”

mentioning

confidence: 99%

Characterization of lectins from wheat seedlings infected with Fusarium graminearum and treated by jasmonic acid

Molodchenkova¹,

Ryshchakova²,

Картузова³

et al. 2023

Ukr.Biochem.J.

View full text Add to dashboard Cite

Fusarium head blight is one of the most serious diseases of wheat caused by a range of Fusarium fungi, which infects the heads of the crop, reducing grain yield. Lectins that specifically bind carbohydrate ligands of various chemical nature and Jasmonic acid (JA) as a key regulator of plant development play an important role in plant protective responses to biotic factors. The goal of the study was to determine the activity and biochemical characteristics of soluble lectins in wheat seedlings of varieties. ‘Lastivka odeska’ with a high resiliency to Fusarium graminearum and ‘Nikonia odeska’ susceptible to Fusarium graminearum. Wheat seedlings were grown on the media containing pathogenic infection or JA solution. Lectins were purified by affinity chromatography and separated by electrophoresis in 15% PAGE. Lectin activity was determined by the method of trypsinized blood erythrocytes hemagglutination. Molecular mass of the main components of lectins from ‘Lastivka odeska’ seedlings was determined to be 67, 60, 45 kDa, and of the main component of lectins from ‘Nikonia odeska’ seedlings – 45 kDa. Lectins isolated from the control untreated seedlings had preferential affinity for N-acetylglucosamine, D-galactosamine and D-fructose-6-phosphate. It was shown that both at pathogen action or JA treatment lectin activity in the seedlings of resistant ‘Lastivka odeska’ variety was increased while in the seedlings of susceptible ‘Nikonia odeska’ variety it was decreased as compared to control. At the joint action of pathogen and JA lectin activity in the seedlings of susceptible variety increased compared with the infected seedlings. The results obtained can be used for development of biochemical methods for assessing the degree of wheat varieties resiliency to fusariose. Keywords: affinity to carbohydrates, Fusarium graminearum, jasmonic acid, resiliency to fusariose, soluble lectins, wheat variety

show abstract

Purification and characterization of a highly thermostable GlcNAc-binding lectin from Collaea speciosa seeds

Cited by 4 publications

References 61 publications

A new lectin from Crotalaria incana seeds and studies of toxicity in Artemia salina nauplii

A new lectin from Crotalaria incana seeds and studies of toxicity in Artemia salina nauplii

Research on the Anti-Tumor Mechanism of Artocarpus Lingnanensis Lectin

Characterization of lectins from wheat seedlings infected with Fusarium graminearum and treated by jasmonic acid

Contact Info

Product

Resources

About