Amoebiasis vaccine development: A snapshot on E. histolytica with emphasis on perspectives of Gal/GalNAc lectin

Singh, Ram Sarup; Walia, Amandeep; Kanwar, Jagat R.; Kennedy, John F.

doi:10.1016/j.ijbiomac.2016.05.043

Cited by 30 publications

(16 citation statements)

References 119 publications

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“…The utility of GalNAc-specific lectins has been reported by several research groups. Gal/GalNAc-specific lectin is a vaccine candidate for amoebiasis and a focus of immunogenicity studies [ 9 ]. Wisteria floribunda agglutinin (WFA), a GalNAc-specific lectin, shows promise for cancer biomarker detection, with disaccharide LacdiNAc (β- d -GalNAc-[1→4]- d -GlcNAc) recognition properties [ 10 ].…”

Section: Introductionmentioning

confidence: 99%

Functional Expression and Characterization of the Recombinant N-Acetyl-Glucosamine/N-Acetyl-Galactosamine-Specific Marine Algal Lectin BPL3

et al. 2018

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Lectins, characterized by their carbohydrate-binding ability, have extensive practical applications. However, their industrial use is limited due to impurity. Thus, quality-controlled production of recombinant lectin is necessary. In this study, the algal lectin BPL3 (Bryopsis plumosa lectin 3) was successfully produced using a bacterial expression system, BL21(DE3), with an artificial repeated structure (dimeric construct). Recombinant dimeric BPL3 (rD2BPL3) was confirmed by LC-MS/MS spectrometry. Expression efficiency was greater for the construct with the repeat structure (rD2BPL3) than the monomeric form (rD1BPL3). Optimal conditions for expression were 1 mM IPTG at 20 °C. Recombinant lectin was purified under denaturing conditions and refolded by the flash dilution method. Recombinant BPL3 was solubilized in 1× PBS containing 2 M urea. rD2BPL3 showed strong hemagglutination activity using human erythrocyte. rD2BPL3 had a similar sugar specificity to that of the native protein, i.e., to N-acetyl-glucosamine (GlcNAc) and N-acetyl-galactosamine (GalNAc). Glycan array results showed that recombinant BPL3 and native BPL3 exhibited different binding properties. Both showed weak binding activity to α-Man-Sp. Native BPL3 showed strong binding specificity to the alpha conformation of amino sugars, and rD2BPL3 had binding activity to the beta conformation. The process developed in this study was suitable for the quality-controlled large-scale production of recombinant lectins.

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Section: Introductionmentioning

confidence: 99%

Functional Expression and Characterization of the Recombinant N-Acetyl-Glucosamine/N-Acetyl-Galactosamine-Specific Marine Algal Lectin BPL3

et al. 2018

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“…[14,15] have been widely reported. Lectins from diverse sources are involved in cell-cell/hostpathogen interactions and trigger many of reactions [16][17][18]. They possess the ability to induce agglutination of cells and have been explored for their biomedical potential [19].…”

Section: Introductionmentioning

confidence: 99%

Antioxidant and antimicrobial activities of Penicillium sp. lectins

Singh

Walia

2019

ARCH BIOL SCI BELGRA

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Lectins are a diverse group of proteins of non-immune origin that interact specifically with glycans. Owing to their specificity, they can mediate various cellular and molecular recognition processes. To explore information on biological activities of lectins from Penicillium duclauxii, P. proteolyticum and P. griseoroseum, they were investigated for their antioxidant and antimicrobial activities. Penicillium sp. lectins exhibited moderate antioxidant activity. P. duclauxii, P. proteolyticum and P. griseoroseum lectins inhibited DPPH with an IC 50 value of 71.42, 75.04 and 82.11 µg/mL, respectively. P. duclauxii, P. proteolyticum and P. griseoroseum lectins inhibited the hydrogen peroxide radical with IC 50 values of 198.57, 209.76 and 215.31 µg/mL, respectively. P. duclauxii and P. proteolyticum lectins exhibited potent antibacterial activity against Gram-negative bacteria. P. griseoroseum lectin inhibited only Gram-positive bacteria. Penicillium sp. lectins did not exhibit antifungal activity. The biological potential of Penicillium sp. lectins will help to understand their biomedical applications. This is the first report on the antioxidant and antimicrobial activities of purified lectins from Penicillium sp.

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“…Entamoeba histolytica is the protozoan responsible for human amoebiasis that infects 50 million people and kills between 30 and 100 thousand individuals around the world (Singh et al, 2016 ). Amoebiasis is characterized by acute diarrhea due to the substantial damage of the colonic epithelium produced by E. histolytica trophozoites (Cornick and Chadee, 2017 ).…”

Section: Introductionmentioning

confidence: 99%

Epithelial Cells Expressing EhADH, An Entamoeba histolytica Adhesin, Exhibit Increased Tight Junction Proteins

Betanzos

Zanatta

Bañuelos

et al. 2018

Front. Cell. Infect. Microbiol.

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In Entamoeba histolytica, the EhADH adhesin together with the EhCP112 cysteine protease, form a 124 kDa complex named EhCPADH. This complex participates in trophozoite adherence, phagocytosis and cytolysis of target cells. EhCPADH and EhCP112 are both involved on epithelium damage, by opening tight junctions (TJ) and reaching other intercellular junctions. EhADH is a scaffold protein belonging to the ALIX family that contains a Bro1 domain, expresses at plasma membrane, endosomes and cytoplasm of trophozoites, and is also secreted to the medium. Contribution of EhADH to TJ opening still remains unknown. In this paper, to elucidate the role of EhADH on epithelium injury, we followed two strategies: producing a recombinant protein (rEhADH) and transfecting the ehadh gene in MDCK cells. Results from the first strategy revealed that rEhADH reached the intercellular space of epithelial cells and co-localized with claudin-1 and occludin at TJ region; later, rEhADH was mainly internalized by clathrin-coated vesicles. In the second strategy, MDCK cells expressing EhADH (MDCK-EhADH) showed the adhesin at plasma membrane. In addition, MDCK-EHADH cells exhibited adhesive features, producing epithelial aggregation and adherence to erythrocytes, as described in trophozoites. Surprisingly, the adhesin expression produced an increase of claudin-1, occludin, ZO-1 and ZO-2 at TJ, and also the transepithelial electric resistance (TEER), which is a measure of TJ gate function. Moreover, MDCK-EhADH cells resulted more susceptible to trophozoites attack, as showed by TEER and cytopathic experiments. Overall, our results indicated that EhADH disturbed TJ from the extracellular space and also intracellularly, suggesting that EhADH affects by itself TJ proteins, and possibly synergizes the action of other parasite molecules during epithelial invasion.

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Amoebiasis vaccine development: A snapshot on E. histolytica with emphasis on perspectives of Gal/GalNAc lectin

Cited by 30 publications

References 119 publications

Functional Expression and Characterization of the Recombinant N-Acetyl-Glucosamine/N-Acetyl-Galactosamine-Specific Marine Algal Lectin BPL3

Functional Expression and Characterization of the Recombinant N-Acetyl-Glucosamine/N-Acetyl-Galactosamine-Specific Marine Algal Lectin BPL3

Antioxidant and antimicrobial activities of Penicillium sp. lectins

Epithelial Cells Expressing EhADH, An Entamoeba histolytica Adhesin, Exhibit Increased Tight Junction Proteins

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