Interaction of Escherichia coli heat-labile enterotoxin B-pentamer with exopolysaccharides from Leuconostoc mesenteroides P35:: Insights from surface plasmon resonance and molecular docking studies

Mojtaba Azari-Anpar; Pascal  Degraeve; Nadia  Oulahal; Isabelle  Adt; Kambiz  Jahanbin; Yann  Demarigny; Ali  Assifaoui; Farideh  Tabatabaei Yazdi

doi:10.1016/j.fbio.2022.102058

Interaction of Escherichia coli heat-labile enterotoxin B-pentamer with exopolysaccharides from Leuconostoc mesenteroides P35: Insights from surface plasmon resonance and molecular docking studies

Mojtaba Azari-Anpar, Pascal Degraeve, Nadia Oulahal, Isabelle Adt, Kambiz Jahanbin, Yann Demarigny, Ali Assifaoui, Farideh Tabatabaei Yazdi^*

^*Corresponding author for this work

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

4 Citations (Scopus)

Abstract

In this study, the interaction of exopolysaccharides from Leuconostoc mesenteroides P35 (EPS-LM) with Escherichia coli heat-labile enterotoxin B-pentamer (LTB) was investigated at different concentrations and temperatures by using surface plasmon resonance (SPR) and molecular docking approaches. FT-IR spectral analysis together with HPTLC analysis revealing that glucose is the only constitutive monosaccharide of EPS-LM suggests that its structure is composed of dextran with α-D (1 → 6) glycosidic linkages. SPR analysis revealed the high affinity of EPS-LM for immobilized LTB toxin (K _A=(2.05 ± 0.04) × 10 ⁶ mol.L ⁻¹ at 37°C). The binding process was spontaneous (ΔG<0), endothermic (ΔH>0), and entropy-driven (ΔS>0) with an increase of K _A with temperature. This suggests that EPS-LM - LTB interaction is dominated by hydrophobic forces. The binding affinity of EPS-LM to LTB had negligible dependence on enthalpy (ΔH = 0.084 kJ mol ⁻¹). Further, molecular docking results suggested the presence of some binding sites of EPS-LM on the LTB through hydrophobic forces (Lys, Asp, Arg, Glu) and also hydrogen bonding (Glu) in the hydrophobic core of LTB. Besides autodock studies, Schiffer-Edmundson helical wheel diagrams of LTB in α-helix domain suggested that LTB hydrophobic core is a highly effective region, which was able to form favorable non-polar interactions of the protein's binding surface (with amino acids residues such as Tyr, Leu, Ile) with EPS-LM. This study provided thus further insights into the interactions between EPS-LM and LTB, suggesting that EPS produced by some LAB, such as EPS produced by Ln. mesenteroides P35 strain are good candidates to inhibit E. coli toxin activity.

Original language	English
Article number	102058
Journal	Food Bioscience
Volume	50
Issue	Part A
Number of pages	10
ISSN	2212-4292
DOIs	https://doi.org/10.1016/j.fbio.2022.102058
Publication status	Published - Dec 2022
Externally published	Yes

Keywords

Detoxification
Escherichia coli heat-labile enterotoxin
Exopolysaccharide
Interaction
Surface plasmon resonance

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10.1016/j.fbio.2022.102058

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Azari-Anpar, M., Degraeve, P., Oulahal, N., Adt, I., Jahanbin, K., Demarigny, Y., Assifaoui, A., & Tabatabaei Yazdi, F. (2022). Interaction of Escherichia coli heat-labile enterotoxin B-pentamer with exopolysaccharides from Leuconostoc mesenteroides P35: Insights from surface plasmon resonance and molecular docking studies. Food Bioscience, 50(Part A), Article 102058. https://doi.org/10.1016/j.fbio.2022.102058

@article{ef95d8b6926e4ba2a722b7571d80bb79,

title = "Interaction of Escherichia coli heat-labile enterotoxin B-pentamer with exopolysaccharides from Leuconostoc mesenteroides P35:: Insights from surface plasmon resonance and molecular docking studies",

abstract = "In this study, the interaction of exopolysaccharides from Leuconostoc mesenteroides P35 (EPS-LM) with Escherichia coli heat-labile enterotoxin B-pentamer (LTB) was investigated at different concentrations and temperatures by using surface plasmon resonance (SPR) and molecular docking approaches. FT-IR spectral analysis together with HPTLC analysis revealing that glucose is the only constitutive monosaccharide of EPS-LM suggests that its structure is composed of dextran with α-D (1 → 6) glycosidic linkages. SPR analysis revealed the high affinity of EPS-LM for immobilized LTB toxin (K A=(2.05 ± 0.04) × 10 6 mol.L −1 at 37°C). The binding process was spontaneous (ΔG<0), endothermic (ΔH>0), and entropy-driven (ΔS>0) with an increase of K A with temperature. This suggests that EPS-LM - LTB interaction is dominated by hydrophobic forces. The binding affinity of EPS-LM to LTB had negligible dependence on enthalpy (ΔH = 0.084 kJ mol −1). Further, molecular docking results suggested the presence of some binding sites of EPS-LM on the LTB through hydrophobic forces (Lys, Asp, Arg, Glu) and also hydrogen bonding (Glu) in the hydrophobic core of LTB. Besides autodock studies, Schiffer-Edmundson helical wheel diagrams of LTB in α-helix domain suggested that LTB hydrophobic core is a highly effective region, which was able to form favorable non-polar interactions of the protein's binding surface (with amino acids residues such as Tyr, Leu, Ile) with EPS-LM. This study provided thus further insights into the interactions between EPS-LM and LTB, suggesting that EPS produced by some LAB, such as EPS produced by Ln. mesenteroides P35 strain are good candidates to inhibit E. coli toxin activity.",

keywords = "Detoxification, Escherichia coli heat-labile enterotoxin, Exopolysaccharide, Interaction, Surface plasmon resonance",

author = "Mojtaba Azari-Anpar and Pascal Degraeve and Nadia Oulahal and Isabelle Adt and Kambiz Jahanbin and Yann Demarigny and Ali Assifaoui and {Tabatabaei Yazdi}, Farideh",

year = "2022",

month = dec,

doi = "10.1016/j.fbio.2022.102058",

language = "English",

volume = "50",

journal = "Food Bioscience",

issn = "2212-4292",

publisher = "Elsevier Ltd",

number = "Part A",

}

Azari-Anpar, M, Degraeve, P, Oulahal, N, Adt, I, Jahanbin, K, Demarigny, Y, Assifaoui, A & Tabatabaei Yazdi, F 2022, 'Interaction of Escherichia coli heat-labile enterotoxin B-pentamer with exopolysaccharides from Leuconostoc mesenteroides P35: Insights from surface plasmon resonance and molecular docking studies', Food Bioscience, vol. 50, no. Part A, 102058. https://doi.org/10.1016/j.fbio.2022.102058

Interaction of Escherichia coli heat-labile enterotoxin B-pentamer with exopolysaccharides from Leuconostoc mesenteroides P35: Insights from surface plasmon resonance and molecular docking studies. / Azari-Anpar, Mojtaba; Degraeve, Pascal ; Oulahal, Nadia et al.
In: Food Bioscience, Vol. 50, No. Part A, 102058, 12.2022.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

TY - JOUR

T1 - Interaction of Escherichia coli heat-labile enterotoxin B-pentamer with exopolysaccharides from Leuconostoc mesenteroides P35:

T2 - Insights from surface plasmon resonance and molecular docking studies

AU - Azari-Anpar, Mojtaba

AU - Degraeve, Pascal

AU - Oulahal, Nadia

AU - Adt, Isabelle

AU - Jahanbin, Kambiz

AU - Demarigny, Yann

AU - Assifaoui, Ali

AU - Tabatabaei Yazdi, Farideh

PY - 2022/12

Y1 - 2022/12

N2 - In this study, the interaction of exopolysaccharides from Leuconostoc mesenteroides P35 (EPS-LM) with Escherichia coli heat-labile enterotoxin B-pentamer (LTB) was investigated at different concentrations and temperatures by using surface plasmon resonance (SPR) and molecular docking approaches. FT-IR spectral analysis together with HPTLC analysis revealing that glucose is the only constitutive monosaccharide of EPS-LM suggests that its structure is composed of dextran with α-D (1 → 6) glycosidic linkages. SPR analysis revealed the high affinity of EPS-LM for immobilized LTB toxin (K A=(2.05 ± 0.04) × 10 6 mol.L −1 at 37°C). The binding process was spontaneous (ΔG<0), endothermic (ΔH>0), and entropy-driven (ΔS>0) with an increase of K A with temperature. This suggests that EPS-LM - LTB interaction is dominated by hydrophobic forces. The binding affinity of EPS-LM to LTB had negligible dependence on enthalpy (ΔH = 0.084 kJ mol −1). Further, molecular docking results suggested the presence of some binding sites of EPS-LM on the LTB through hydrophobic forces (Lys, Asp, Arg, Glu) and also hydrogen bonding (Glu) in the hydrophobic core of LTB. Besides autodock studies, Schiffer-Edmundson helical wheel diagrams of LTB in α-helix domain suggested that LTB hydrophobic core is a highly effective region, which was able to form favorable non-polar interactions of the protein's binding surface (with amino acids residues such as Tyr, Leu, Ile) with EPS-LM. This study provided thus further insights into the interactions between EPS-LM and LTB, suggesting that EPS produced by some LAB, such as EPS produced by Ln. mesenteroides P35 strain are good candidates to inhibit E. coli toxin activity.

AB - In this study, the interaction of exopolysaccharides from Leuconostoc mesenteroides P35 (EPS-LM) with Escherichia coli heat-labile enterotoxin B-pentamer (LTB) was investigated at different concentrations and temperatures by using surface plasmon resonance (SPR) and molecular docking approaches. FT-IR spectral analysis together with HPTLC analysis revealing that glucose is the only constitutive monosaccharide of EPS-LM suggests that its structure is composed of dextran with α-D (1 → 6) glycosidic linkages. SPR analysis revealed the high affinity of EPS-LM for immobilized LTB toxin (K A=(2.05 ± 0.04) × 10 6 mol.L −1 at 37°C). The binding process was spontaneous (ΔG<0), endothermic (ΔH>0), and entropy-driven (ΔS>0) with an increase of K A with temperature. This suggests that EPS-LM - LTB interaction is dominated by hydrophobic forces. The binding affinity of EPS-LM to LTB had negligible dependence on enthalpy (ΔH = 0.084 kJ mol −1). Further, molecular docking results suggested the presence of some binding sites of EPS-LM on the LTB through hydrophobic forces (Lys, Asp, Arg, Glu) and also hydrogen bonding (Glu) in the hydrophobic core of LTB. Besides autodock studies, Schiffer-Edmundson helical wheel diagrams of LTB in α-helix domain suggested that LTB hydrophobic core is a highly effective region, which was able to form favorable non-polar interactions of the protein's binding surface (with amino acids residues such as Tyr, Leu, Ile) with EPS-LM. This study provided thus further insights into the interactions between EPS-LM and LTB, suggesting that EPS produced by some LAB, such as EPS produced by Ln. mesenteroides P35 strain are good candidates to inhibit E. coli toxin activity.

KW - Detoxification

KW - Escherichia coli heat-labile enterotoxin

KW - Exopolysaccharide

KW - Interaction

KW - Surface plasmon resonance

U2 - 10.1016/j.fbio.2022.102058

DO - 10.1016/j.fbio.2022.102058

M3 - Journal article

SN - 2212-4292

VL - 50

JO - Food Bioscience

JF - Food Bioscience

IS - Part A

M1 - 102058

ER -

Interaction of Escherichia coli heat-labile enterotoxin B-pentamer with exopolysaccharides from Leuconostoc mesenteroides P35: Insights from surface plasmon resonance and molecular docking studies

Abstract

Keywords

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