Purification,Biochemical Characterization,and Amino Acid Sequence of a Novel Type of Lectin from <Emphasis Type="Italic">Aplysia dactylomela</Emphasis> Eggs with Antibacterial/Antibiofilm Potential |
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Authors: | Rômulo Farias Carneiro Renato Cézar Farias Torres Renata Pinheiro Chaves Mayron Alves de Vasconcelos Bruno Lopes de Sousa André Castelo Rodrigues Goveia Francisco Vassiliepe Arruda Maria Nágila Carneiro Matos Helena Matthews-Cascon Valder Nogueira Freire Edson Holanda Teixeira Celso Shiniti Nagano Alexandre Holanda Sampaio |
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Institution: | 1.Laboratório de Biotecnologia Marinha – BioMar-Lab, Departamento de Engenharia de Pesca,Universidade Federal do Ceará,Fortaleza,Brazil;2.Laboratório Integrado de Biomoléculas - LIBS, Departamento de Patologia e Medicina Legal,Universidade Federal do Ceará,Fortaleza,Brazil;3.Departamento de Física,Universidade Federal do Ceará,Fortaleza,Brazil;4.Laboratório de Invertebrados Marinhos do Ceará – LIMCE, Departamento de Biologia,Universidade Federal do Ceará,Fortaleza,Brazil |
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Abstract: | A new lectin from Aplysia dactylomela eggs (ADEL) was isolated by affinity chromatography on HCl-activated Sepharose? media. Hemagglutination caused by ADEL was inhibited by several galactosides, mainly galacturonic acid (Ka = 6.05 × 106 M?1). The primary structure of ADEL consists of 217 residues, including 11 half-cystines involved in five intrachain and one interchain disulfide bond, resulting in a molecular mass of 57,228 ± 2 Da, as determined by matrix-assisted laser desorption/ionization time of flight mass spectrometry. ADEL showed high similarity with lectins isolated from Aplysia eggs, but not with other known lectins, indicating that these lectins could be grouped into a new family of animal lectins. Three glycosylation sites were found in its polypeptide backbone. Data from peptide-N-glycosidase F digestion and MS suggest that all oligosaccharides attached to ADEL are high in mannose. The secondary structure of ADEL is predominantly β-sheet, and its tertiary structure is sensitive to the presence of ligands, as observed by CD. A 3D structure model of ADEL was created and shows two domains connected by a short loop. Domain A is composed of a flat three-stranded and a curved five-stranded β-sheet, while domain B presents a flat three-stranded and a curved four-stranded β-sheet. Molecular docking revealed favorable binding energies for interactions between lectin and galacturonic acid, lactose, galactosamine, and galactose. Moreover, ADEL was able to agglutinate and inhibit biofilm formation of Staphylococcus aureus, suggesting that this lectin may be a potential alternative to conventional use of antimicrobial agents in the treatment of infections caused by Staphylococcal biofilms. |
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