Publications by authors named "Renato Cezar Farias Torres"

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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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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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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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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