Evidence map›Paper›PMID 30443878›Full record

ArticleCell stress & chaperones2019

Induced expression of small heat shock proteins is associated with thermotolerance in female Laodelphax striatellus planthoppers.

Lihua Wang, Yueliang Zhang, Lei Pan, Qin Wang, Yangchun Han, Hongtao Niu, Dan Shan, Ary Hoffmann, Jichao Fang

Abstract read
In one paragraph

Article in Cell stress & chaperones, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Spatiotemporal Patterns of Five Small Heat Shock Protein Genes inInternational journal of molecular sciences · 2023
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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.

Lihua Wang *Institute of Plant Protection, Jiangsu Academy of Agricultural Sciences, Key Laboratory of Food Quality and Safety of Jiangsu Province-State Key Laboratory Breeding Base, Nanjing, 210014, China. yangwlh@163.com.ORCID http://orcid.org/0000-0002-9204-9850
Yueliang Zhang *Institute of Plant Protection, Jiangsu Academy of Agricultural Sciences, Key Laboratory of Food Quality and Safety of Jiangsu Province-State Key Laboratory Breeding Base, Nanjing, 210014, China.
Lei PanInstitute of Plant Protection, Jiangsu Academy of Agricultural Sciences, Key Laboratory of Food Quality and Safety of Jiangsu Province-State Key Laboratory Breeding Base, Nanjing, 210014, China.
Qin WangSuzhou Academy of Agricultural Sciences, Suzhou, 215155, China.
Yangchun HanInstitute of Plant Protection, Jiangsu Academy of Agricultural Sciences, Key Laboratory of Food Quality and Safety of Jiangsu Province-State Key Laboratory Breeding Base, Nanjing, 210014, China.
Hongtao NiuInstitute of Plant Protection, Jiangsu Academy of Agricultural Sciences, Key Laboratory of Food Quality and Safety of Jiangsu Province-State Key Laboratory Breeding Base, Nanjing, 210014, China.
Dan ShanInstitute of Plant Protection, Jiangsu Academy of Agricultural Sciences, Key Laboratory of Food Quality and Safety of Jiangsu Province-State Key Laboratory Breeding Base, Nanjing, 210014, China.
Ary HoffmannBio21 Institute, School of BioSciences, The University of Melbourne, Melbourne, VIC, 3010, Australia.
Jichao FangInstitute of Plant Protection, Jiangsu Academy of Agricultural Sciences, Key Laboratory of Food Quality and Safety of Jiangsu Province-State Key Laboratory Breeding Base, Nanjing, 210014, China. fangjc126@126.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Insects are often exposed to high temperature stress in natural environments, but the mechanisms involved in thermotolerance in many insect groups like Hemiptera are not well known. To explore possible mechanisms of thermotolerance in the hemipteran pest Laodelphax striatellus, which damages rice through direct feeding and viral transmission, small heat shock proteins (sHsps) implicated in thermotolerance in other insect groups were identified. The seven sHsps identified have a conserved alpha crystallin domain, a variable N-terminal region, and shared relative low identities to each other. Three of the sHsp genes (LsHsp20.5, LsHsp21.5, and LsHsp21.6) exhibited higher basal expression than the other four genes but showed weak or no heat-induced expression. The other four genes (LsHsp20.1, LsHsp21.2, LsHsp21.4, and LsHsp22.0) were induced up to 3306-fold by heat. Injection of dsRNA indicated that expression of these sHsps was associated with thermotolerance, and Escherichia coli transformed with LsHsp21.2 and LsHsp20.1 showed relatively higher thermotolerance. These results point to an important functional role of these sHsps for thermotolerance in L. striatellus.

Indexed as

ThermotoleranceAmino Acid SequenceAnimalsEscherichia coliFemaleGene Expression ProfilingHeat-Shock Proteins, SmallHemipteraInsect ProteinsPhylogenyRNA, Double-StrandedHeat-Shock Proteins, SmallInsect ProteinsRNA, Double-StrandedExpressionLaodelphax striatellussHspsStressThermotolerance

Identifiers

PMID30443878
PMCPMC6363632

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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.