ArticleApplied and environmental microbiology2014
Adaptation of the wine bacterium Oenococcus oeni to ethanol stress: role of the small heat shock protein Lo18 in membrane integrity.
Article in Applied and environmental microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 65 citations in OpenAlex.
- Impact of N-terminal domain on the sHSP Lo18 function.Scientific reports · 2025Article
- Unveiling the Potential of Lentilactobacillus hilgardii in Malolactic Fermentation: Comparative Genomics and Fermentation Dynamics.Microbial biotechnology · 2025Article
- A microaerobically induced small heat shock protein contributes toApplied and environmental microbiology · 2025Article
- The role of membrane physiology in sHSP Lo18-lipid interaction and lipochaperone activity.Scientific reports · 2024Article
- Deletions of conserved extracytoplasmic function sigma factors-encoding genes in Streptomyces have a major impact on secondary metabolism.Microbial cell factories · 2024Article
- Significant influence of four highly conserved amino-acids in lipochaperon-active sHsps on the structure and functions of the Lo18 protein.Scientific reports · 2023Article
- Molecular chaperone function of three small heat-shock proteins from a model probiotic species.Cell stress & chaperones · 2023Article
- Is the lipochaperone activity of sHSP a key to the stress response encoded in its primary sequence?Cell stress & chaperones · 2023Review
- Genomic Analysis of an Excellent Wine-Making StrainPolish journal of microbiology · 2022Article
- Exploring the diversity of bacteriophage specific to Oenococcus oeni and Lactobacillus spp and their role in wine production.Applied microbiology and biotechnology · 2021Review
- The Small Ones Matter-sHsps in the Bacterial Chaperone Network.Frontiers in molecular biosciences · 2021Review
- Effect of exogenous proline on the ethanolic tolerance and malolactic performance ofJournal of food science and technology · 2020Article
- Small but mighty: a functional look at bacterial sHSPs.Cell stress & chaperones · 2020Review
- Heterologous Expression of Argininosuccinate Synthase FromFrontiers in microbiology · 2019Article
- Relative expression of stress-related genes during acclimation at low temperature of psychrotrophic Oenococcus oeni strains from Patagonian wine.World journal of microbiology & biotechnology · 2018Article
- Heterologous expression of Oenococcus oeni sHSP20 confers temperature stress tolerance in Escherichia coli.Cell stress & chaperones · 2018Article
- CtsR, the Master Regulator of Stress-Response inFrontiers in microbiology · 2018Article
- Article
- Transcriptome responses of Lactobacillus acetotolerans F28 to a short and long term ethanol stress.Scientific reports · 2017Article
- Stress Physiology of Lactic Acid Bacteria.Microbiology and molecular biology reviews : MMBR · 2016Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Malolactic fermentation in wine is often carried out by Oenococcus oeni. Wine is a stressful environment for bacteria because ethanol is a toxic compound that impairs the integrity of bacterial membranes. The small heat shock protein (sHsp) Lo18 is an essential actor of the stress response in O. oeni. Lo18 prevents the thermal aggregation of proteins and plays a crucial role in membrane quality control. Here, we investigated the interaction between Lo18 and four types of liposomes: one was prepared from O. oeni grown under optimal growth conditions (here, control liposomes), one was prepared from O. oeni grown in the presence of 8% ethanol (here, ethanol liposomes), one was prepared from synthetic phospholipids, and one was prepared from phospholipids from Bacillus subtilis or Lactococcus lactis. We observed the strongest interaction between Lo18 and control liposomes. The lipid binding activity of Lo18 required the dissociation of oligomeric structures into dimers. Protein protection experiments carried out in the presence of the liposomes from O. oeni suggested that Lo18 had a higher affinity for control liposomes than for a model protein. In anisotropy experiments, we mimicked ethanol action by temperature-dependent fluidization of the liposomes. Results suggest that the principal determinant of Lo18-membrane interaction is lipid bilayer phase behavior rather than phospholipid composition. We suggest a model to describe the ethanol adaptation of O. oeni. This model highlights the dual role of Lo18 in the protection of proteins from aggregation and membrane stabilization and suggests how modifications of phospholipid content may be a key factor determining the balance between these two functions.
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