TY - JOUR
T1 - Antibacterial activity of a new lectin isolated from the marine sponge Chondrilla caribensis
AU - Marques, Dayara Normando
AU - Almeida, Alexandra Sampaio de
AU - Sousa, Andressa Rocha de Oliveira
AU - Pereira, Rafael
AU - Andrade, Alexandre Lopes
AU - Chaves, Renata Pinheiro
AU - Carneiro, Rômulo Farias
AU - Vasconcelos, Mayron Alves de
AU - Nascimento-Neto, Luiz Gonzaga do
AU - Pinheiro, Ulisses
AU - Videira, Paula Alexandra
AU - Teixeira, Edson Holanda
AU - Nagano, Celso Shiniti
AU - Sampaio, Alexandre Holanda
N1 - sem pdf conforme despacho
PY - 2018/4/1
Y1 - 2018/4/1
N2 - 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.
AB - 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.
KW - Antibacterial
KW - Antibiofilm
KW - Lectin
UR - http://www.scopus.com/inward/record.url?scp=85035095028&partnerID=8YFLogxK
U2 - 10.1016/j.ijbiomac.2017.11.140
DO - 10.1016/j.ijbiomac.2017.11.140
M3 - Article
C2 - 29175164
AN - SCOPUS:85035095028
SN - 0141-8130
VL - 109
SP - 1292
EP - 1301
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
ER -