Inhibition of quorum sensing and biofilm in Pseudomonas aeruginosa by erythrinin B: Bioinformatic evidence for the LasR binding
Abstract
Quorum sensing (QS)-regulated virulence factors and biofilm formation are major contributors to antimicrobial resistance in Pseudomonas aeruginosa. This highlights the urgent need for novel anti-virulence strategies that can disrupt these pathways and reduce such infections. The objective of this study was to evaluate the inhibitory potential of erythrinin B against QS-regulated virulence factors and biofilm formation in P. aeruginosa PAO1. Erythrinin B significantly suppressed pyocyanin (72.27%), pyoverdin (68.22%), protease (83.08%), and elastase (62.16%) production in a dose-dependent manner, while rhamnolipid inhibition was lesser (29.17%). Biofilm biomass was reduced by 73.02% at 300 μg/mL, corroborated by microscopy, which revealed diminished adherence and scattered planktonic cells. EPS (exopolysaccharides) and alginate levels were also markedly decreased, indicating disruption of biofilm matrix integrity. Molecular docking demonstrated that erythrinin B binds to LasR receptor (−11.7 kcal/mol), forming hydrogen bonds with Thr75, Tyr56, Tyr64, and Ser129, alongside hydrophobic and van der Waals contacts. MD simulations confirmed the stability of complex, with minor conformational changes compared to apo LasR. MM/GBSA analysis revealed favourable binding energy (−26.89 ± 2.04 kcal/mol), dominated by van der Waals interactions, with key contributions from Val76, Trp88, and Leu36. These findings indicate erythrinin B as potent QS inhibitor that attenuates virulence and biofilm formation in P. aeruginosa.
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BibTeX
@article{alohali2026inhibition,
title = {{Inhibition of quorum sensing and biofilm in Pseudomonas aeruginosa by erythrinin B: Bioinformatic evidence for the LasR binding}},
author = {Basim M. Alohali and Fohad Mabood Husain and Nasser A. Al-Shabib and Mohammed A. Alshuniaber},
journal = {Frontiers in Microbiology},
year = {2026},
month = nov,
doi = {10.3389/fmicb.2026.1954689},
url = {https://www.frontiersin.org/articles/10.3389/fmicb.2026.1954689},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Inhibition of quorum sensing and biofilm in Pseudomonas aeruginosa by erythrinin B: Bioinformatic evidence for the LasR binding
AU - Basim M. Alohali
AU - Fohad Mabood Husain
AU - Nasser A. Al-Shabib
AU - Mohammed A. Alshuniaber
PY - 2026
DA - 2026/11/06
JO - Frontiers in Microbiology
DO - 10.3389/fmicb.2026.1954689
UR - https://www.frontiersin.org/articles/10.3389/fmicb.2026.1954689
AB - Quorum sensing (QS)-regulated virulence factors and biofilm formation are major contributors to antimicrobial resistance in Pseudomonas aeruginosa. This highlights the urgent need for novel anti-virulence strategies that can disrupt these pathways and reduce such infections. The objective of this study was to evaluate the inhibitory potential of erythrinin B against QS-regulated virulence factors and biofilm formation in P. aeruginosa PAO1. Erythrinin B significantly suppressed pyocyanin (72.27%), pyoverdin (68.22%), protease (83.08%), and elastase (62.16%) production in a dose-dependent manner, while rhamnolipid inhibition was lesser (29.17%). Biofilm biomass was reduced by 73.02% at 300 μg/mL, corroborated by microscopy, which revealed diminished adherence and scattered planktonic cells. EPS (exopolysaccharides) and alginate levels were also markedly decreased, indicating disruption of biofilm matrix integrity. Molecular docking demonstrated that erythrinin B binds to LasR receptor (−11.7 kcal/mol), forming hydrogen bonds with Thr75, Tyr56, Tyr64, and Ser129, alongside hydrophobic and van der Waals contacts. MD simulations confirmed the stability of complex, with minor conformational changes compared to apo LasR. MM/GBSA analysis revealed favourable binding energy (−26.89 ± 2.04 kcal/mol), dominated by van der Waals interactions, with key contributions from Val76, Trp88, and Leu36. These findings indicate erythrinin B as potent QS inhibitor that attenuates virulence and biofilm formation in P. aeruginosa.
SN - 1664-302X
ER -