A small HSP, Lo18, interacts with the cell membrane and modulates lipid physical state under heat shock conditions in a lactic acid bacterium

Coucheney, Françoise; Gal, Laurent; Beney, Laurent; Lherminier, Jeannine; Gervais, Patrick; Guzzo, Jean

doi:10.1016/j.bbamem.2005.11.017

Cited by 71 publications

(70 citation statements)

References 32 publications

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“…In the lactic acid bacterium O. oeni, the sHsp Lo18 is mostly associated with the membranes when the cells are heat-shocked or treated with ethanol or BA which can disturb membranes (Coucheney et al 2005). It also seems that Lo18 can modulate membrane properties by increasing its molecular order, which leads to a diminished membrane fluidity.…”

Section: Possible Mechanism Of Hsp Protection and Potential Therapeutmentioning

confidence: 99%

Alcohol stress, membranes, and chaperones

Tóth

Vı́gh

Sántha

2014

Cell Stress and Chaperones

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Ethanol, which affects all body organs, exerts a number of cytotoxic effects, most of them independent of cell type. Ethanol treatment leads to increased membrane fluidity and to changes in membrane protein composition. It can also interact directly with membrane proteins, causing conformational changes and thereby influencing their function. The cytotoxic action may include an increased level of oxidative stress. Heat shock protein molecular chaperones are ubiquitously expressed evolutionarily conserved proteins which serve as critical regulators of cellular homeostasis. Heat shock proteins can be induced by various forms of stresses such as elevated temperature, alcohol treatment, or ischemia, and they are also upregulated in certain pathological conditions. As heat shock and ethanol stress provoke similar responses, it is likely that heat shock protein activation also has a role in the protection of membranes and other cellular components during alcohol stress.

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Section: Possible Mechanism Of Hsp Protection and Potential Therapeutmentioning

confidence: 99%

Alcohol stress, membranes, and chaperones

Tóth

Vı́gh

Sántha

2014

Cell Stress and Chaperones

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“…Under stress conditions O. oeni produces large amounts of the sHsp Lo18 (2)(3)(4)25), particularly during ethanol shock (3,26). As it is not yet possible to construct the appropriate mutants in O. oeni or to overexpress the proteins to verify their in vivo function, many studies have been performed with heterologous models (27,28) or in vitro with purified proteins (17).…”

mentioning

confidence: 99%

“…As it is not yet possible to construct the appropriate mutants in O. oeni or to overexpress the proteins to verify their in vivo function, many studies have been performed with heterologous models (27,28) or in vitro with purified proteins (17). In vitro experiments with purified Lo18 have characterized both its molecular chaperone (protection of proteins from aggregation) and lipochaperone (stabilization of liposome fluidity) activities (17,26,29). Recently, we provided strong evidence for a relationship between the dynamic oligomerization of Lo18 and its chaperone and lipochaperone activities (17).…”

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Adaptation of the Wine Bacterium Oenococcus oeni to Ethanol Stress: Role of the Small Heat Shock Protein Lo18 in Membrane Integrity

Maitre¹,

Weidmann²,

Dubois‐Brissonnet

et al. 2014

Appl Environ Microbiol

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cMalolactic 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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“…In Oenococcus oeni, a lactic acid bacterium, an 18-kDa sHsp (Lo18) is induced by several stresses such as heat or ethanol, and it is associated with the membrane after ethanol treating. This sHsp has a direct effect on the phospholipids and modulates the membrane properties by increasing their molecular order, which decreases the membrane fluidity (Coucheney et al 2005). The Hsp60 GroEL was also shown to increase the molecular order of lipid bilayers and stabilize the membrane under stress conditions (Török et al 1997).…”

Section: Discussionmentioning

confidence: 99%

Neuroprotective effect of small heat shock protein, Hsp27, after acute and chronic alcohol administration

Tóth

Gonda

Vı́gh

et al. 2010

Cell Stress and Chaperones

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Alcohol induces degeneration of neurons and inhibits neurogenesis in the brain. Small heat shock proteins are able to protect neurons in cerebral ischemia and oxidative stress. In this study, we investigated the neuroprotective effect of small heat shock protein, Hsp27, after acute and chronic ethanol administrations using transgenic mice overexpressing the human Hsp27 protein.Transgenic mice and wild-type littermates were injected with 2 g/kg ethanol intraperitoneally, and then motor coordination and muscle strength were analyzed using different behavioral tests, such as footprint analysis, balance beam, and inverted screen tests. Ethanol-injected transgenic mice showed similar footprints to control salineinjected mice, did not fall of the beam, and were able to climb to the top of the inverted screen, while wild-type mice showed ataxia and incoordination after ethanol injection. The effect of Hsp27 on chronic ethanol consumption was also investigated. Drinking water of mice was replaced by a 20% ethanol solution for 5 weeks, and then brain sections were stained with Fluoro Jade C staining. We found significantly lesser amount of degenerating neurons in the brain of ethanol-drinking transgenic mice compared to wild-type mice. We conclude that Hsp27 can protect neurons against the acute and chronic toxic effects of ethanol.

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A small HSP, Lo18, interacts with the cell membrane and modulates lipid physical state under heat shock conditions in a lactic acid bacterium

Cited by 71 publications

References 32 publications

Alcohol stress, membranes, and chaperones

Alcohol stress, membranes, and chaperones

Adaptation of the Wine Bacterium Oenococcus oeni to Ethanol Stress: Role of the Small Heat Shock Protein Lo18 in Membrane Integrity

Neuroprotective effect of small heat shock protein, Hsp27, after acute and chronic alcohol administration

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