A new mucin-binding lectin from the marine sponge Aplysina fulva (AFL) exhibits antibiofilm effects

Autor: Mayron Alves de Vasconcelos, Ulisses Pinheiro, Lídia Torquato da Silva, Rômulo Farias Carneiro, Alexandre Lopes Andrade, Jhonatas Teixeira Viana, Alexandre Holanda Sampaio, Renato Cézar Farias Torres, Edson Holanda Teixeira, Celso Shiniti Nagano
Rok vydání: 2019
Předmět:
Zdroj: Archives of Biochemistry and Biophysics. 662:169-176
ISSN: 0003-9861
Popis: A new mucin-binding lectin (AFL) was isolated from the marine sponge Aplysina fulva. AFL was purified by affinity chromatography on Sepharose™ matrix. Its hemagglutinating activity was independent of divalent ions, and it was weakly inhibited by simple sugars. However, porcine stomach mucin was a powerful inhibitor. In SDS PAGE, piridylethylated AFL showed one band of approximately 16 kDa, whereas in the non-reducing conditions, AFL showed at least two bands of 30 and 70 kDa. Mass spectrometry MALDI-ToF analysis showed one major ion of 31,652 ± 5 Da, which corresponded to a dimer formed by subunits linked by disulfide bonds. The first fifteen amino acids of AFL were determined, and no sequence similarity was observed with any known protein. Internal sequences were obtained by mass spectrometry analysis of tryptic digestion of AFL spots. These peptides showed similarity with a lectin from marine sponge Aplysina lactuca. Secondary structure of AFL was predominantly formed by β-conformations, which were stable at variations of pH and temperature. AFL did not inhibit planktonic growth of Gram-positive and Gram-negative bacteria tested. However, the lectin did significantly reduce the biomass biofilm of the bacteria Staphylococcus aureus, S. epidermidis, and Escherichia coli.
Databáze: OpenAIRE