Title
Antibacterial activity of a new lectin isolated from the marine sponge Chondrilla caribensis
Author
Dayara NormandoMarques, Alexandra Sampaio de Almeida, Andressa Rocha de Oliveira Sousa, Rafael Pereira, Alexandre Lopes Andrade, Renata Pinheiro Chaves, Rômulo Farias Carneiro, Mayron Alves de Vasconcelos, Luiz Gonzaga do Nascimento-Neto, Ulisses Pinheiro, Paula Alexandra Videira, Edson Holanda Teixeira, Celso Shiniti Nagano, Alexandre Holanda Sampaio
Year
2017
Journal
International Journal of Biological Macromolecules
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 disaccharidescontaining 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 CarbohydrateRecognition Domain (CRD) of the lectin was involved in antibiofilm activity.
Instrument
J-815
Keywords
Circular dichroism, Secondary structure, Tertiary structure, Chemical stability, Thermal stability, Biochemistry