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

• Published in: International journal of biological macromolecules Vol. 109; pp. 1292 - 1301
• Main Authors: 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
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01-04-2018
• Subjects: Antibacterial; Antibiofilm; Lectin; Lectin; Antibiofilm; Antibacterial
• ISSN: 0141-8130; 1879-0003
• DOI: 10.1016/j.ijbiomac.2017.11.140

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.