ArticleScientific reports2024
The role of membrane physiology in sHSP Lo18-lipid interaction and lipochaperone activity.
Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Impact of N-terminal domain on the sHSP Lo18 function.Scientific reports · 2025Article
- Review
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5 authors.
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Abstract
To cope with environmental stresses, organisms, including lactic acid bacteria such as O. oeni, produce stress proteins called HSPs. In wine, O. oeni is constantly confronted by stress affecting its membrane fluidity. To survive through in these deleterious conditions, O. oeni synthesizes Lo18, a unique, small HSP which acts as a molecular chaperone and a lipochaperone. The molecular mechanism underlying its lipochaperone activity, particularly regarding membrane lipid composition, remains poorly understood. In this context, Lo18 lipochaperone activity and the associated modification in protein structure were studied during interaction with different liposomes from O. oeni cultures representing unstressed, stressed and stressed-adapted physiological states. The results showed that the presence of the membrane (whatever its nature) induces a modification of Lo18's structure. Also, the presence of oleic acid and/or phosphatidylglycerol is important to favor Lo18-membrane interaction, allowing lipochaperone activity. This research enhances understanding of sHSP-membrane interactions in bacterial systems.
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