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

Carneiro, Rômulo Farias; Viana, Jhonatas Teixeira; Torres, Renato Cézar Farias; Silva, Lídia Torquato da; Andrade, Alexandre Lopes; Vasconcelos, Mayron Alves de; Pinheiro, Ulisses; Teixeira, Edson Holanda; Nagano, Celso Shiniti; Sampaio, Alexandre Holanda

doi:10.1016/j.abb.2018.12.014

Cited by 14 publications

(7 citation statements)

References 30 publications

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“…After exposing GYL to various pH values for 1 h, we noted the optimal range of pH to be in the alkaline zone ( Figure 3 a). Increases in HA accompanied by increases in pH are also characteristic of the lectins of many invertebrates—for example, lectin from the marine sponge Aplysina fulva [ 39 ], the clam R. philippinarum [ 38 ], and the mussel Crenomytilus grayanus [ 40 ]. Regarding temperature, GYL retained its HA up to 20 °C; however, HA dramatically decreased at temperatures above this.…”

Section: Resultsmentioning

confidence: 99%

Identification and Characterization of a Novel Lectin from the Clam Glycymeris yessoensis and Its Functional Characterization under Microbial Stimulation and Environmental Stress

et al. 2021

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Lectin from the bivalve Glycymeris yessoensis (GYL) was purified by affinity chromatography on porcine stomach mucin–Sepharose. GYL is a dimeric protein with a molecular mass of 36 kDa, as established by SDS-PAGE and MALDI-TOF analysis, consisting of 18 kDa subunits linked by a disulfide bridge. According to circular dichroism data, GYL is a β/α-protein with the predominance of β-structure. GYL preferentially agglutinates enzyme-treated rabbit erythrocytes and recognizes glycoproteins containing O-glycosidically linked glycans, such as porcine stomach mucin (PSM), fetuin, thyroglobulin, and ovalbumin. The amino acid sequences of five segments of GYL were acquired via mass spectrometry. The sequences have no homology with other known lectins. GYL is Ca2+-dependent and stable over a range above a pH of 8 and temperatures up to 20 °C for 30 min. GYL is a pattern recognition receptor, as it binds common pathogen-associated molecular patterns, such as peptidoglycan, LPS, β-1,3-glucan and mannan. GYL possesses a broad microbial-binding spectrum, including Gram-positive (Bacillus subtilis, Staphylococcus aureus) and Gram-negative bacteria (Escherichia coli, Vibrio proteolyticus), but not the fungus Candida albicans. Expression levels of GYL in the hemolymph were significantly upregulated after bacterial challenge by V. proteolyticus plus environmental stress (diesel fuel). Results indicate that GYL is probably a new member of the C-type lectin family, and may be involved in the immune response of G. yessoensis to bacterial attack.

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Section: Resultsmentioning

confidence: 99%

Identification and Characterization of a Novel Lectin from the Clam Glycymeris yessoensis and Its Functional Characterization under Microbial Stimulation and Environmental Stress

et al. 2021

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“…IsL has also been inhibited by PSM, which is an O-linked glycoprotein containing galactose, GalNac and fucose residues (Devine & Harada 1991). Lectins from Aplysina lactuca (ALL) and A. fulva (AFL) were also inhibited by galactose containing-carbohydrates and glycoprotein PSM (Carneiro et al 2019, Carneiro et al 2017a). However, unlike IsL, ALL and AFL showed low affinity for simple carbohydrates.…”

Section: Discussionmentioning

confidence: 99%

“…was able to function as mammalian ionotropic glutamate receptors (Ueda et al 2013); CCL from Chondrilla caribensis showed leshimanicide effect (Sousa et al 2021); lectins from Cinachyrella appion and Haliclona caerulea showed pro apoptotic effect against human cervical adenocarcinoma cells and human breast cancer cells, respectively (Rabelo et al 2012, Nascimento-Neto et al 2018. Moreover, lectins from Aplysna lactuca and A. fulva were able to reduce bacterial biofilms (Carneiro et al 2019(Carneiro et al , 2017a.…”

Section: Introductionmentioning

confidence: 99%

Purification, biochemical characterization of a lectin from marine sponge Ircinia strobilina and its effect on the inhibition of bacterial biofilms

ALMEIDA,

MENDONÇA,

CARNEIRO

et al. 2023

An. Acad. Bras. Ciênc.

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A new lectin from marine sponge Ircinia strobilina, denominated IsL, was isolated by combination of affinity chromatography in Guar gum matrix followed by size exclusion chromatography. IsL was able to agglutinate native and enzymatically treated rabbit erythrocytes, being inhibited by galactosides, such as α-methyl-Dgalactopyranoside, β-methyl-D-galactopyranoside and α-lactose. IsL hemagglutinating activity was stable at neutral to alkaline pH, however the lectin loses its activity at 40° C.The molecular mass determinated by mass spectrometry was 13.655 ± 5 Da. Approximately 40% of the primary structure of IsL was determined by mass spectrometry, but no similarity was observed with any protein. The secondary structure of IsL consists of 28% α-helix, 26% β-sheet, and 46% random region, as determined by dichroism circular. IsL was a calcium-dependent lectin, but no significant variations were observed by circular dichroism when IsL was incubated in presence of calcium and EDTA. IsL was not toxic against Artemia nauplii and did not have antimicrobial activity against bacterial cells. However, the IsL was able to significantly inhibit the biofilm formation of Staphylococcus aureus and Staphylococcus epidermidis.

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“…Furthermore, a lectin isolated from Chinese shrimp inhibited Gram-negative and Gram-positive bacteria such as K. pneunomiae, E. coli, S. aureus, M. The marine sponge Aplysina fulva mucin-binding lectin displayed a secondary structure formed by pH-stable and thermostable β-conformations and structural resemblance to a lectin from another marine sponge A. lactuca. The lectin reduced the biomass of the biofilm of the bacteria E. coli, S. aureus, and S. epidermidis but was devoid of a suppressive effect on planktonic growth of Gram-negative bacteria and Gram-positive bacteria examined [64]. N-acetyl hexosamine-binding Japanese black sponge (Halichondria okadai) lectin expressed growth suppressing activity toward a fungus (A. niger), Gram-negative bacteria (E. coli, P. aeruginosa, and S. boydii), and a Gram-positive bacterium (L. monocytogenes).…”

Section: Antibacterial Activitymentioning

confidence: 95%

“…The lectin reduced the biomass of the biofilm of the bacteria E. coli , S . aureus , and S. epidermidis but was devoid of a suppressive effect on planktonic growth of Gram-negative bacteria and Gram-positive bacteria examined [ 64 ]. N -acetyl hexosamine-binding Japanese black sponge ( Halichondria okadai ) lectin expressed growth suppressing activity toward a fungus ( A. niger ), Gram-negative bacteria ( E. coli , P .…”

Section: Other Biological Activities Of Lectinsmentioning

confidence: 99%

An Update of Lectins from Marine Organisms: Characterization, Extraction Methodology, and Potential Biofunctional Applications

et al. 2022

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Lectins are a unique group of nonimmune carbohydrate-binding proteins or glycoproteins that exhibit specific and reversible carbohydrate-binding activity in a non-catalytic manner. Lectins have diverse sources and are classified according to their origins, such as plant lectins, animal lectins, and fish lectins. Marine organisms including fish, crustaceans, and mollusks produce a myriad of lectins, including rhamnose binding lectins (RBL), fucose-binding lectins (FTL), mannose-binding lectin, galectins, galactose binding lectins, and C-type lectins. The widely used method of extracting lectins from marine samples is a simple two-step process employing a polar salt solution and purification by column chromatography. Lectins exert several immunomodulatory functions, including pathogen recognition, inflammatory reactions, participating in various hemocyte functions (e.g., agglutination), phagocytic reactions, among others. Lectins can also control cell proliferation, protein folding, RNA splicing, and trafficking of molecules. Due to their reported biological and pharmaceutical activities, lectins have attracted the attention of scientists and industries (i.e., food, biomedical, and pharmaceutical industries). Therefore, this review aims to update current information on lectins from marine organisms, their characterization, extraction, and biofunctionalities.

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

Cited by 14 publications

References 30 publications

Identification and Characterization of a Novel Lectin from the Clam Glycymeris yessoensis and Its Functional Characterization under Microbial Stimulation and Environmental Stress

Identification and Characterization of a Novel Lectin from the Clam Glycymeris yessoensis and Its Functional Characterization under Microbial Stimulation and Environmental Stress

Purification, biochemical characterization of a lectin from marine sponge Ircinia strobilina and its effect on the inhibition of bacterial biofilms

An Update of Lectins from Marine Organisms: Characterization, Extraction Methodology, and Potential Biofunctional Applications

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