Evidence map›Paper›PMID 36417097›Full record

ArticleCell stress & chaperones2023

Molecular chaperone function of three small heat-shock proteins from a model probiotic species.

Maria Teresa Rocchetti, Tiffany Bellanger, Maria Incoronata Trecca, Stephanie Weidmann, Rosella Scrima, Giuseppe Spano, Pasquale Russo, Vittorio Capozzi, Daniela Fiocco

Abstract read
In one paragraph

Article in Cell stress & chaperones, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed.

  1. Review
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  3. Lactic acid bacterial strains isolated fromFrontiers in microbiology · 2026
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Maria Teresa RocchettiDepartment of Clinical and Experimental Medicine, University of Foggia, Via Pinto 1, 71122, Foggia, Italy.
Tiffany BellangerUniv. Bourgogne, Franche-Comté, AgroSup Dijon, PAM UMR A 02.102, Dijon, France.
Maria Incoronata TreccaDepartment of Clinical and Experimental Medicine, University of Foggia, Via Pinto 1, 71122, Foggia, Italy.
Stephanie WeidmannUniv. Bourgogne, Franche-Comté, AgroSup Dijon, PAM UMR A 02.102, Dijon, France.
Rosella ScrimaDepartment of Clinical and Experimental Medicine, University of Foggia, Via Pinto 1, 71122, Foggia, Italy.
Giuseppe SpanoDepartment of Agriculture Food Natural Science Engineering (DAFNE), University of Foggia, Via Napoli 25, 71122, Foggia, Italy.
Pasquale RussoDepartment of Agriculture Food Natural Science Engineering (DAFNE), University of Foggia, Via Napoli 25, 71122, Foggia, Italy.
Vittorio CapozziInstitute of Sciences of Food Production, National Research Council (CNR) of Italy, C/O CS-DAT, Via Michele Protano, 71122, Foggia, Italy.
Daniela FioccoDepartment of Clinical and Experimental Medicine, University of Foggia, Via Pinto 1, 71122, Foggia, Italy. daniela.fiocco@unifg.it.ORCID 0000-0002-3654-0362

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small heat-shock proteins (sHSP) are ubiquitous ATP-independent chaperones that prevent irreversible aggregation of heat-damaged denaturing proteins. Lactiplantibacillus plantarum is a widespread Gram-positive bacterium with probiotic claims and vast potential for agro-food, biotechnological and biomedical applications. L. plantarum possesses a family of three sHSP, which were previously demonstrated to be involved in its stress tolerance mechanisms. Here, the three L. plantarum sHSP were heterologously expressed, purified and shown to have a chaperone activity in vitro, measuring their capacity to suppress protein aggregation, as assayed spectrophotometrically by light scattering. Their anti-aggregative capacity was found to be differently influenced by pH. Differences were also found relative to their holdase function and their capacity to modulate liposome membrane fluidity, suggesting interplays between them and indicating diversified activities. This is the first study assessing the chaperone action of sHSP from a probiotic model. The different roles of the three sHSP can increase L. plantarum's capabilities to survive the various types of stress characterising the diverse habitats of this highly adaptable species. Reported evidence supports the interest in L. plantarum as one of the model species for bacteria that have three different sHSP-encoding genes in their genomes.

Indexed as

Bacterial ProteinsHeat-Shock Proteins, SmallLactobacillaceaeMolecular ChaperonesBacterial ProteinsHeat-Shock Proteins, SmallMolecular ChaperonesHeat stressHoldaseLipochaperoneMembrane fluidityProtein aggregationsHSP

Identifiers

PMID36417097
PMCPMC9877261

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.