Purification, Biochemical Characterization, and Amino Acid Sequence of a Novel Type of Lectin from Aplysia dactylomela Eggs with Antibacterial/Antibiofilm Potential

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 × 10 6 M −1 ). The primary structure of ADEL consists of 217 residu...

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Bibliographic Details
Published in:	Marine biotechnology (New York, N.Y.) Vol. 19; no. 1; pp. 49 - 64
Main Authors:	Carneiro, Rômulo Farias, Torres, Renato Cézar Farias, Chaves, Renata Pinheiro, de Vasconcelos, Mayron Alves, de Sousa, Bruno Lopes, Goveia, André Castelo Rodrigues, Arruda, Francisco Vassiliepe, Matos, Maria Nágila Carneiro, Matthews-Cascon, Helena, Freire, Valder Nogueira, Teixeira, Edson Holanda, Nagano, Celso Shiniti, Sampaio, Alexandre Holanda
Format:	Journal Article
Language:	English
Published:	New York Springer US 01-02-2017 Springer Nature B.V
Subjects:	Amino Acid Sequence Amino acids Animals Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - isolation & purification Anti-Bacterial Agents - metabolism Anti-Bacterial Agents - pharmacology Antimicrobial agents Aplysia - chemistry Aplysia - genetics Aplysia - metabolism Aplysia dactylomela Biofilms Biofilms - drug effects Biofilms - growth & development Biomedical and Life Sciences Chromatography Eggs Engineering Escherichia coli - genetics Escherichia coli - metabolism Freshwater & Marine Ecology Galactosides - pharmacology Gene Expression Hemagglutination Inhibition Tests Hexuronic Acids - pharmacology Ionization Ions Lactose Lectins Lectins - chemistry Lectins - genetics Lectins - isolation & purification Lectins - pharmacology Life Sciences Marine Mass spectrometry Microbiology Molecular Docking Simulation Mollusks Original Article Protein Domains Protein Structure, Secondary Proteins Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - pharmacology Scientific imaging Sequence Alignment Staphylococcus aureus Staphylococcus aureus - drug effects Staphylococcus aureus - growth & development Zoology Zygote - chemistry Biofilm Lectin Galacturonic acid Sea hare Mass spectrometry
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Summary:	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 × 10 6 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.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1436-2228 1436-2236
DOI:	10.1007/s10126-017-9728-x