Isolation, biochemical characterization and antibiofilm effect of a lectin from the marine sponge Aplysina lactuca

被引：16
作者：
Carneiro, Romulo Farias [1 ]
Pinheiro de Lima, Paulo Henrique, Jr. [1 ]
Chaves, Renata Pinheiro [1 ]
Pereira, Rafael [2 ]
Pereira, Anna Luisa [2 ]
de Vasconcelos, Mayron Alves [2 ]
Pinheiro, Ulisses [3 ]
Teixeira, Edson Holanda [2 ]
Nagano, Celso Shiniti [1 ]
Sampaio, Alexandre Holanda [1 ]
机构：
[1] Univ Fed Ceara, Dept Engn Pesca, Lab Biotecnol Marinha BioMar Lab, Campus Pici S-N,Bloco 871, BR-60440970 Fortaleza, Ceara, Brazil
[2] Univ Fed Ceara, Dept Patol & Med Legal, Lab Integrado Biomol LIBS, Monsenhor Furtado S-N, BR-60430160 Fortaleza, Ceara, Brazil
[3] UFPE Univ Fed Pernambuco, Dept Zool, Av Prof Moraes Rego 1235,Cidade Univ, BR-50670901 Recife, PE, Brazil
来源：
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2017年 / 99卷
关键词：
Mass spectrometry; Protein characterization; Lectin; Sponge; Purification; Circular dichroism; PROTEIN SECONDARY STRUCTURE; AMINO-ACID-SEQUENCE; AXINELLA-POLYPOIDES; CLIONA-VARIANS; BINDING LECTIN; PURIFICATION; INVERTEBRATES; AGGREGATION; DIVERSITY; EXTRACTS;
D O I：
10.1016/j.ijbiomac.2017.02.020
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
A new lectin was isolated from the marine sponge Aplysina lactuca (ALL) by combining ammonium sulfate precipitation and affinity chromatography on guar gum matrix. ALL showed affinity for the disaccharides alpha-lactose, beta-lactose and lactulose (Ka = 12.5,31.9 and 145.5 M-1, respectively), as well as the glycoprotein porcine stomach mucin. Its hemagglutinating activity was stable in neutral acid pH values and temperatures below 60 degrees C. ALL is a dimeric protein formed by two covalently linked polypeptide chains. The average molecular mass, as determined by Electrospray Ionization Mass Spectrometry (ESI-MS), was 31,810 +/- 2 Da. ESI-MS data also indicated the presence of three cysteines involved in one intrachain and one interchain disulfide bond. The partial amino acid sequence of ALL was determined by tandem mass spectrometry. Eight tryptic peptides presented similarity with lectin I isolated from Axinella polypoides. Its secondary structure is predominantly beta-sheet, as indicated by circular dichroism (CD) spectroscopy. ALL agglutinated gram-positive and gram-negative bacterial cells, and it were able to significantly reduce the biomass of the bacterial biofilm tested at dose- dependent effect. (C) 2017 Elsevier B.V. All rights reserved.
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页码：213 / 222
页数：10
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