Characterization of novel lectins from Burkholderia pseudomallei and Chromobacterium violaceum with seven-bladed β-propeller fold

Sýkorová, Petra; Novotná, Jitka; Demo, Gabriel; Pompidor, Guillaume; Dubská, Eva; Komárek, Jan; Fujdiarová, Eva; Houser, Josef; Hároníková, Lucia; Varrot, A.; Shilova, Nadezhda V.; Bovin, Nicolai V.; Pokorná, Martina; Wimmerová, Michaela

doi:10.1016/j.ijbiomac.2019.10.200

Cited by 6 publications

(2 citation statements)

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“…Lectins are disparate ubiquitous proteins distributed in a conventional order among microorganisms, plants, and animals, containing at least one non-enzymatic domain enabling them to descry in reversible selective comportment to specific sugars or carbohydrate-associated structures without modifying the arrangement of the bound carbohydrates [14] , [15] , [16] , [17] . Advances in bio-techniques and genome-wide screenings of plant lectins have unraveled the multitude of different lectin sequences within single plant species suggesting their exploitation for biotechnological purposes [18] .…”

Section: Introductionmentioning

confidence: 99%

Purification and erythrocyte-membrane perturbing activity of a ketose-specific lectin from Moringa oleifera seeds

Nubi

Adewole²,

Agunbiade

et al. 2021

Biotechnology Reports

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Highlights Purification of Moringa oleifera seed lectin (MoL) was achieved by ammonium sulfate precipitation and size exclusion chromatography MoL hemagglutinating activity was thermostable up to 90°C, within pH 2-4 and moderately inhibited by sucrose and fructose Traces of Ca2+, Mg2+, and Na+ was detected in MoL, and modification of arginine and tryptophan residues affected the hemagglutinating activity Hemolytic (membrane-perturbing) activity of MoL was potentiated in mildly acidic pH, and dependent on concentration, temperature, pH, and time of incubation.

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Section: Introductionmentioning

confidence: 99%

Purification and erythrocyte-membrane perturbing activity of a ketose-specific lectin from Moringa oleifera seeds

Nubi

Adewole²,

Agunbiade

et al. 2021

Biotechnology Reports

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“…Glycan microarrays can be tailored to carry relevant structures or patterns providing high-throughput information on protein-carbohydrate interactions using a small amount of sample (Geissner, Anish, & Seeberger, 2014;Geissner et al, 2019;Martinez et al, 2020). The identification of carbohydrate ligands for a range of proteins, toxins and whole bacteria have been performed in past years for several species and specific proteins like Burkholderia lectins (Audfray et al, 2012;Sýkorov a et al, 2020;De Oliveira et al, 2017;Day et al, 2015;Deng et al, 2014).…”

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confidence: 99%

Burkholderia cenocepacia BCAM2418‐induced antibody inhibits bacterial adhesion, confers protection to infection and enables identification of host glycans as adhesin targets

Pimenta

Kilcoyne

Bernardes

et al. 2021

Cellular Microbiology

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Trimeric Autotransporter Adhesins (TAA) found in Gram-negative bacteria play a key role in virulence. This is the case of Burkholderia cepacia complex (Bcc), a group of related bacteria able to cause infections in patients with cystic fibrosis. These bacteria use TAAs, among other virulence factors, to bind to host protein receptors and their carbohydrate ligands. Blocking such contacts is an attractive approach to inhibit Bcc infections. In this study, using an antibody produced against the TAA BCAM2418 from the epidemic strain Burkholderia cenocepacia K56-2, we were able to uncover its roles as an adhesin and the type of host glycan structures that serve as recognition targets. The neutralisation of BCAM2418 was found to cause a reduction in the adhesion of the bacteria to bronchial cells and mucins. Moreover, in vivo studies have shown that the anti-BCAM2418 antibody exerted an inhibitory effect during infection in Galleria mellonella. Finally, inferred by glycan arrays, we were able to predict for the first time, host glycan epitopes for a TAA. We show that BCAM2418 favoured binding to 3 0 sialyl-3-fucosyllactose, histo-blood group A, α-(1,2)-linked Fuccontaining structures, Lewis structures and GM1 gangliosides. In addition, the glycan microarrays demonstrated similar specificities of Burkholderia species for their most intensely binding carbohydrates. K E Y W O R D S adhesin antibody, Burkholderia cepacia complex, host glycans as adhesin targets, trimeric autotransporter adhesins 1 | INTRODUCTION Members of the denominated Burkholderia cepacia complex (Bcc; group of 22 species), can cause severe infections in humans and animals (Scoffone et al., 2017). Among those, Burkholderia cenocepacia and Burkholderia multivorans are particularly dangerous for cystic fibrosis (CF) patients (Scoffone et al., 2017). They are highly adapted

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One, two, many: Strategies to alter the number of carbohydrate binding sites of lectins

Tobola

Wiltschi

2022

Biotechnology Advances

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Characterization of novel lectins from Burkholderia pseudomallei and Chromobacterium violaceum with seven-bladed β-propeller fold

Cited by 6 publications

References 58 publications

Purification and erythrocyte-membrane perturbing activity of a ketose-specific lectin from Moringa oleifera seeds

Purification and erythrocyte-membrane perturbing activity of a ketose-specific lectin from Moringa oleifera seeds

Burkholderia cenocepacia BCAM2418‐induced antibody inhibits bacterial adhesion, confers protection to infection and enables identification of host glycans as adhesin targets

One, two, many: Strategies to alter the number of carbohydrate binding sites of lectins

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