Antibacterial activity of a new lectin isolated from the marine sponge Chondrilla caribensis

Dayara Normando Marques, Alexandra Sampaio de Almeida, Andressa Rocha de Oliveira Sousa, Rafael Pereira, Alexandre Lopes Andrade, Renata Pinheiro Chaves, Rômulo Farias Carneiro, Mayron Alves de Vasconcelos, Luiz Gonzaga do Nascimento-Neto, Ulisses Pinheiro, Paula Alexandra Videira, Edson Holanda Teixeira, Celso Shiniti Nagano, Alexandre Holanda Sampaio

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

A new lectin from the marine sponge Chondrilla caribensis (CCL) was isolated by affinity chromatography in Sepharose 6B media. CCL is a homotetrameric protein formed by subunits of 15,445 ±2 Da. The lectin showed affinity for disaccharides containing galactose and mucin. Mass spectrometric analysis revealed about 50% of amino acid sequence of CCL, which showed similarity with a lectin isolated from Aplysina lactuca. Secondary structure consisted of 10% α-helix, 74% β-sheet/β-turn and 16% coil, and this profile was unaltered in a broad range of pH and temperatures. CCL agglutinated Staphylococcus aureus, S epidermidis and Escherichia coli, and it was able to reduce biofilm biomass, but showed no inhibition of planktonic growth of these bacteria. CCL activity was inhibited by α-lactose, indicating that Carbohydrate Recognition Domain (CRD) of the lectin was involved in antibiofilm activity.

Original languageEnglish
Pages (from-to)1292-1301
Number of pages10
JournalInternational Journal of Biological Macromolecules
Volume109
DOIs
Publication statusPublished - 1 Apr 2018

Fingerprint

Porifera
Lectins
Affinity chromatography
Disaccharides
Protein Subunits
Biofilms
Mucins
Lactose
Carbohydrates
Galactose
Affinity Chromatography
Biomass
Sepharose
Escherichia coli
Staphylococcus aureus
Amino acids
Amino Acid Sequence
Bacteria
Proteins
Amino Acids

Keywords

  • Antibacterial
  • Antibiofilm
  • Lectin

Cite this

Marques, D. N., Almeida, A. S. D., Sousa, A. R. D. O., Pereira, R., Andrade, A. L., Chaves, R. P., ... Sampaio, A. H. (2018). Antibacterial activity of a new lectin isolated from the marine sponge Chondrilla caribensis. International Journal of Biological Macromolecules, 109, 1292-1301. https://doi.org/10.1016/j.ijbiomac.2017.11.140
Marques, Dayara Normando ; Almeida, Alexandra Sampaio de ; Sousa, Andressa Rocha de Oliveira ; Pereira, Rafael ; Andrade, Alexandre Lopes ; Chaves, Renata Pinheiro ; Carneiro, Rômulo Farias ; Vasconcelos, Mayron Alves de ; Nascimento-Neto, Luiz Gonzaga do ; Pinheiro, Ulisses ; Videira, Paula Alexandra ; Teixeira, Edson Holanda ; Nagano, Celso Shiniti ; Sampaio, Alexandre Holanda. / Antibacterial activity of a new lectin isolated from the marine sponge Chondrilla caribensis. In: International Journal of Biological Macromolecules. 2018 ; Vol. 109. pp. 1292-1301.
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abstract = "A new lectin from the marine sponge Chondrilla caribensis (CCL) was isolated by affinity chromatography in Sepharose 6B media. CCL is a homotetrameric protein formed by subunits of 15,445 ±2 Da. The lectin showed affinity for disaccharides containing galactose and mucin. Mass spectrometric analysis revealed about 50{\%} of amino acid sequence of CCL, which showed similarity with a lectin isolated from Aplysina lactuca. Secondary structure consisted of 10{\%} α-helix, 74{\%} β-sheet/β-turn and 16{\%} coil, and this profile was unaltered in a broad range of pH and temperatures. CCL agglutinated Staphylococcus aureus, S epidermidis and Escherichia coli, and it was able to reduce biofilm biomass, but showed no inhibition of planktonic growth of these bacteria. CCL activity was inhibited by α-lactose, indicating that Carbohydrate Recognition Domain (CRD) of the lectin was involved in antibiofilm activity.",
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Marques, DN, Almeida, ASD, Sousa, ARDO, Pereira, R, Andrade, AL, Chaves, RP, Carneiro, RF, Vasconcelos, MAD, Nascimento-Neto, LGD, Pinheiro, U, Videira, PA, Teixeira, EH, Nagano, CS & Sampaio, AH 2018, 'Antibacterial activity of a new lectin isolated from the marine sponge Chondrilla caribensis', International Journal of Biological Macromolecules, vol. 109, pp. 1292-1301. https://doi.org/10.1016/j.ijbiomac.2017.11.140

Antibacterial activity of a new lectin isolated from the marine sponge Chondrilla caribensis. / Marques, Dayara Normando; Almeida, Alexandra Sampaio de; Sousa, Andressa Rocha de Oliveira; Pereira, Rafael; Andrade, Alexandre Lopes; Chaves, Renata Pinheiro; Carneiro, Rômulo Farias; Vasconcelos, Mayron Alves de; Nascimento-Neto, Luiz Gonzaga do; Pinheiro, Ulisses; Videira, Paula Alexandra; Teixeira, Edson Holanda; Nagano, Celso Shiniti; Sampaio, Alexandre Holanda.

In: International Journal of Biological Macromolecules, Vol. 109, 01.04.2018, p. 1292-1301.

Research output: Contribution to journalArticle

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T1 - Antibacterial activity of a new lectin isolated from the marine sponge Chondrilla caribensis

AU - Marques, Dayara Normando

AU - Almeida, Alexandra Sampaio de

AU - Sousa, Andressa Rocha de Oliveira

AU - Pereira, Rafael

AU - Andrade, Alexandre Lopes

AU - Chaves, Renata Pinheiro

AU - Carneiro, Rômulo Farias

AU - Vasconcelos, Mayron Alves de

AU - Nascimento-Neto, Luiz Gonzaga do

AU - Pinheiro, Ulisses

AU - Videira, Paula Alexandra

AU - Teixeira, Edson Holanda

AU - Nagano, Celso Shiniti

AU - Sampaio, Alexandre Holanda

N1 - sem pdf conforme despacho

PY - 2018/4/1

Y1 - 2018/4/1

N2 - A new lectin from the marine sponge Chondrilla caribensis (CCL) was isolated by affinity chromatography in Sepharose 6B media. CCL is a homotetrameric protein formed by subunits of 15,445 ±2 Da. The lectin showed affinity for disaccharides containing galactose and mucin. Mass spectrometric analysis revealed about 50% of amino acid sequence of CCL, which showed similarity with a lectin isolated from Aplysina lactuca. Secondary structure consisted of 10% α-helix, 74% β-sheet/β-turn and 16% coil, and this profile was unaltered in a broad range of pH and temperatures. CCL agglutinated Staphylococcus aureus, S epidermidis and Escherichia coli, and it was able to reduce biofilm biomass, but showed no inhibition of planktonic growth of these bacteria. CCL activity was inhibited by α-lactose, indicating that Carbohydrate Recognition Domain (CRD) of the lectin was involved in antibiofilm activity.

AB - A new lectin from the marine sponge Chondrilla caribensis (CCL) was isolated by affinity chromatography in Sepharose 6B media. CCL is a homotetrameric protein formed by subunits of 15,445 ±2 Da. The lectin showed affinity for disaccharides containing galactose and mucin. Mass spectrometric analysis revealed about 50% of amino acid sequence of CCL, which showed similarity with a lectin isolated from Aplysina lactuca. Secondary structure consisted of 10% α-helix, 74% β-sheet/β-turn and 16% coil, and this profile was unaltered in a broad range of pH and temperatures. CCL agglutinated Staphylococcus aureus, S epidermidis and Escherichia coli, and it was able to reduce biofilm biomass, but showed no inhibition of planktonic growth of these bacteria. CCL activity was inhibited by α-lactose, indicating that Carbohydrate Recognition Domain (CRD) of the lectin was involved in antibiofilm activity.

KW - Antibacterial

KW - Antibiofilm

KW - Lectin

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