Evidence map›Paper›PMID 20139186›Full record

ArticleJournal of bacteriology2010

Genetic modification of the Salmonella membrane physical state alters the pattern of heat shock response.

Amalia Porta, Zsolt Török, Ibolya Horvath, Silvia Franceschelli, László Vígh, Bruno Maresca

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.1field-weighted citation impact, top 24% of its field
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

6 citing papers in PubMed, 19 citations in OpenAlex.

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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

6 authors at 3 institutions in 2 countries.

Amalia PortaUniversity of Salerno, Department of Pharmaceutical Sciences, Faculty of Pharmacy, Division of BioMedicine, Salerno, Italy.
Zsolt Török
Ibolya Horvath
Silvia Franceschelli
László Vígh
Bruno Maresca
University of Salerno · ITHUN-REN Szegedi Biológiai Kutatóközpont · HUInstitute of Biochemistry · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

It is now recognized that membranes are not simple physical barriers but represent a complex and dynamic environment that affects membrane protein structures and their functions. Recent data emphasize the role of membranes in sensing temperature changes, and it has been shown that the physical state of the plasma membrane influences the expression of a variety of genes such as heat shock genes. It has been widely shown that minor alterations in lipid membranes are critically involved in the conversion of signals from the environment to the transcriptional activation of heat shock genes. Previously, we have proposed that the composition, molecular arrangement, and physical state of lipid membranes and their organization have crucial roles in cellular responses during stress caused by physical and chemical factors as well as in pathological states. Here, we show that transformation of Salmonella enterica serovar Typhimurium LT2 (Salmonella Typhimurium) with a heterologous Delta(12)-desaturase (or with its trans-membrane regions) causes major changes in the pathogen's membrane dynamic. In addition, this pathogen is strongly impaired in the synthesis of major stress proteins (heat shock proteins) under heat shock. These data support the hypothesis that the perception of temperature in Salmonella is strictly controlled by membrane order and by a specific membrane lipid/protein ratio that ultimately causes transcriptional activation of heat shock genes. These results represent a previously unrecognized mode of sensing temperature variation used by this pathogen at the onset of infection.

Indexed as

Heat-Shock ResponseAnimalsCell LineCell MembraneFatty Acid DesaturasesHeat-Shock ProteinsHot TemperatureMacrophagesMiceRecombinant ProteinsSalmonella typhimuriumdelta-12 fatty acid desaturaseFatty Acid DesaturasesHeat-Shock ProteinsRecombinant Proteins

Identifiers

PMID20139186
PMCPMC2838041
OpenAlexW2103102598

What OpenQuestion holds

Textmetadata
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Registered trials

None linked

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.