| Literature DB >> 29175164 |
Dayara Normando Marques1, Alexandra Sampaio de Almeida1, Andressa Rocha de Oliveira Sousa1, Rafael Pereira2, Alexandre Lopes Andrade2, Renata Pinheiro Chaves1, Rômulo Farias Carneiro1, Mayron Alves de Vasconcelos3, Luiz Gonzaga do Nascimento-Neto4, Ulisses Pinheiro5, Paula Alexandra Videira6, Edson Holanda Teixeira2, Celso Shiniti Nagano1, Alexandre Holanda Sampaio7.
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 ±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.Entities:
Keywords: Antibacterial; Antibiofilm; Lectin
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Year: 2017 PMID： 29175164 DOI： 10.1016/j.ijbiomac.2017.11.140
Source DB: PubMed Journal: Int J Biol Macromol ISSN： 0141-8130 Impact factor: 6.953