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

2017; Elsevier BV; Volume: 109; Linguagem: Inglês

10.1016/j.ijbiomac.2017.11.140

1879-0003

Dayara Normando Marques, 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 dos Santos Pinheiro, Paula A. Videira, Edson Holanda Teixeira, Celso Shiniti Nagano, Alexandre Holanda Sampaio,

Microbial Natural Products and Biosynthesis

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.