Publications by authors named "Celso Shiniti Nagano"

This study aimed to evaluate the antihyperglycemic and antioxidant activities of the lectin isolated from (BTL). Diabetes was induced in Wistar rats through low-dose streptozotocin injections. Following the confirmation of hyperglycaemia, the animals were treated with 150 mM NaCl, glibenclamide, or BTL at 600 or 900 mg/kg.

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Article Synopsis
  • A novel lectin called AcrL was isolated from the marine sponge Aiolochroia crassa, which specifically binds to glycans with sialic acid and shows a typical galectin structure with carbohydrate-binding sites.
  • AcrL demonstrated strong antibacterial effects by inhibiting biofilm formation in bacteria such as Staphylococcus aureus and Escherichia coli, with varying concentrations required for effectiveness.
  • The lectin also enhances the efficacy of antibiotics and damages bacterial membranes, suggesting its potential as a new antibacterial agent in the fight against infections.
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Faced with the emergence of multiresistant microorganisms that affect human health, microbial agents have become a serious global threat, affecting human health and plant crops. Antimicrobial peptides have attracted significant attention in research for the development of new microbial control agents. This work's goal was the structural characterization and analysis of antifungal activity of chitin-binding peptides from and seeds on the growth of and species.

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Lectins presents the ability to interact with glycans and trigger varied responses, including the inhibition of the development of various pathogens. Structural studies of these proteins are essential to better understand their functions. In marine sponges, so far only a few lectins have their primary structures completely determined.

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The SfL-1 isoform from the marine red algae Solieria filiformis was produced in recombinant form (rSfL-1) and showed hemagglutinating activity and inhibition similar to native SfL. The analysis of circular dichroism revealed the predominance of β-strands structures with spectra of βI-proteins for both lectins, which had Melting Temperature (Tm) between 41 °C and 53 °C. The three-dimensional structure of the rSfL-1 was determined by X-ray crystallography, revealing that it is composed of two β-barrel domains formed by five antiparallel β chains linked by a short peptide between the β-barrels.

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Background: Protease inhibitors (PIs) have attracted attention due to their important roles in plant defense.

Objective: The objective of this work was to characterize and evaluate the antimicrobial activity of the peptides of a family of serine PIs from Capsicum chinense Jacq. seeds.

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Fibrinogen-related proteins (FREPs) have been identified in several animals. They are involved in the body's defense, acting as mediators of phagocytosis. Ficolins and intelectins are some of the most studied Fibrinogen-related Domain (FReD)-containing lectins.

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The emergence of antibiotic resistance poses a serious and challenging threat to healthcare systems, making it imperative to discover novel therapeutic options. This work reports the isolation and characterization of a thermostable trypsin inhibitor from chia (Salvia hispanica L.) seeds, with antibacterial activity against Staphylococcus aureus sensitive and resistant to methicillin.

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Inflammation and oxidative stress are processes associated with different human diseases. They are treated using drugs that have several side effects. Seaweed are sources of potentially relevant natural compounds for use as treatment of these disorders.

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Plant fungal diseases cause major problems for the global economy. Antimicrobial peptides have aroused great interest in the control of phytopathogens, as they are natural molecules and have a broad spectrum of inhibitory activity. Herein, we have tried to identify and characterize antimicrobial peptides present in fruits of Capsicum chinense and to evaluate their enzymatic and antifungal activities.

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Article Synopsis
  • * Molecular docking analysis indicated that CCL interacts with carbohydrates in a way similar to other galectins, and it demonstrated significant anti-leishmanial activity by inhibiting the growth of the Leishmania infantum parasite.
  • * CCL is recognized as one of the few sponge lectins with a fully determined primary structure, showing great potential for biotechnological applications, particularly in the fight against diseases like Leishmaniasis.
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Key Message: HO priming reprograms essential proteins' expression to help plants survive, promoting responsive and unresponsive proteins adjustment to salt stress.

Abstacrt: Priming is a powerful strategy to enhance abiotic stress tolerance in plants. Despite this, there is scarce information about the mechanisms induced by HO priming for salt stress tolerance, particularly on proteome modulation.

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The aim of the study was to assess the antihyperglycemic, antilipidemic, and antioxidant effects of a lectin isolated from Bryothamnion seaforthii (BSL), on rats with streptozotocin (STZ)-induced diabetes. The disease model was induced by low-dose injections of STZ. Diabetic rats were treated with NaCl 150 mM, metformin, and BSL at different concentrations.

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The modern pig industry relies on extensive use of artificial insemination with cooled semen. It is important that semen doses maintain their quality during processing, transport and storage before insemination to guarantee maximum fertility rates. However, ejaculates may respond differently to liquid preservation at 17 °C, despite the optimal quality assessed before cooling.

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A new mucin-binding lectin (AFL) was isolated from the marine sponge Aplysina fulva. AFL was purified by affinity chromatography on Sepharose™ matrix. Its hemagglutinating activity was independent of divalent ions, and it was weakly inhibited by simple sugars.

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This study was conducted to evaluate the effects of different feeding levels on the proteome of oviduct and uterus tissues of hormonally stimulated goats during the periovulatory period. Forty goats were separated into four different diet groups: Diet 1.0 M (n = 11), Diet 1.

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A new lectin from the marine sponge Chondrilla caribensis (CCL) was isolated by affinity chromatography in Sepharose 6B media. CCL is a homotetrameric protein formed by subunits of 15,445 ±2Da. The lectin showed affinity for disaccharides containing galactose and mucin.

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As described in the literature, Solieria filiformis lectin (SfL) from the marine red alga S. filiformis was found to have antinociceptive and anti-inflammatory effects. In this study, we characterized two SfL variants, SfL-1 and SfL-2, with molecular mass of 27,552Da and 27,985Da, respectively.

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Lectins are proteins, or glycoproteins, capable of reversibly binding to specific mono- or oligosaccharides via a noncatalytic domain. The Diocleinae subtribe presents lectins with high structural similarity, but different effects based on biological activity assays. This variability results from small structural differences.

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A new lectin was isolated from the marine sponge Aplysina lactuca (ALL) by combining ammonium sulfate precipitation and affinity chromatography on guar gum matrix. ALL showed affinity for the disaccharides α-lactose, β-lactose and lactulose (Ka=12.5, 31.

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A new lectin from Aplysia dactylomela eggs (ADEL) was isolated by affinity chromatography on HCl-activated Sepharose™ media. Hemagglutination caused by ADEL was inhibited by several galactosides, mainly galacturonic acid (Ka = 6.05 × 10 M).

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The three-dimensional structure of Dioclea reflexa seed lectin (DrfL) was studied in detail by a combination of X-ray crystallography, molecular docking and molecular dynamics. DrfL was purified by affinity chromatography using Sephadex G-50 matrix. Its primary structure was obtained by mass spectrometry, and crystals belonging to orthorhombic space group P222 were grown by the vapor diffusion method at 293K.

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A lectin from Canavalia virosa, Diocleinae subtribe, was purified by affinity chromatography with Sephadex G-50 matrix and named ConV. The primary structure of ConV was obtained by mass spectrometry and crystals were obtained by the vapor diffusion method at 293K and belonged to orthorhombic space group P222 with two molecules in its asymmetric unit. The structure obtained presented R and R of 18.

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Legume lectins have been widely studied and applied for many purposes in the last few decades, but many of their physiological aspects remain elusive. The Diocleinae legume subtribe, which includes intensively explored lectins, such as ConA, presents an unusual and extensive post-translational process which results in minor alterations in protein structure, in turn making its function elusive. Despite previous reports about Diocleinae precursor activity, no structural or functional analyses have ever been carried out to understand the impacts of post-translational processing relative to lectin structure and binding specificity.

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A novel lectin from seeds of Clathrotropis nitida (CNA) was purified and characterized. CNA is a glycoprotein containing approximately 3.3% carbohydrates in its structure.

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