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Marques, Dayara Normando; Almeida, Alexandra Sampaio de; Sousa, Andressa Rocha de Oliveira; Pereira, Rafael; Andrade, Alexandre Lopes; Chaves, Renata Pinheiro; Carneiro, Rômulo Farias; Vasconcelos, Mayron Alves de; Nascimento-Neto, Luiz Gonzaga do; Pinheiro, Ulisses; Videira, Paula Alexandra; Teixeira, Edson Holanda; Nagano, Celso Shiniti; Sampaio, Alexandre Holanda
International journal of biological macromolecules, 04/2018, Letnik: 109Journal Article
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. Mass spectrometric analysis revealed about 50% of amino acid sequence of CCL, which showed similarity with a lectin isolated from Aplysina lactuca. Secondary structure consisted of 10% α-helix, 74% β-sheet/β-turn and 16% coil, and this profile was unaltered in a broad range of pH and temperatures. CCL agglutinated Staphylococcus aureus, S epidermidis and Escherichia coli, and it was able to reduce biofilm biomass, but showed no inhibition of planktonic growth of these bacteria. CCL activity was inhibited by α-lactose, indicating that Carbohydrate Recognition Domain (CRD) of the lectin was involved in antibiofilm activity.
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