Antibacterial activity of a new lectin isolated from the marine sponge Chondrilla caribensis

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Abstract

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 ±2 Da. 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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Marques, D. N., Almeida, A. S. de, Sousa, A. R. de O., Pereira, R., Andrade, A. L., Chaves, R. P., … Sampaio, A. H. (2018). Antibacterial activity of a new lectin isolated from the marine sponge Chondrilla caribensis. International Journal of Biological Macromolecules, 109, 1292–1301. https://doi.org/10.1016/j.ijbiomac.2017.11.140

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