Evidence map›Paper›PMID 26655641›Full record

ArticleScientific reports2015

NMR structure and function of Helicoverpa armigera sterol carrier protein-2, an important insecticidal target from the cotton bollworm.

Haihao Ma, Yuemin Ma, Xuehui Liu, David H Dyer, Pingyong Xu, Kaiyu Liu, Que Lan, Huazhu Hong, Jianxin Peng, Rong Peng

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. 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
0.8field-weighted citation impact, top 27% 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

4 citing papers in PubMed, 17 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

10 authors at 5 institutions in 2 countries.

Haihao MaSchool of Life Sciences, Central China Normal University, Wuhan, P.R.China.
Yuemin MaSchool of Life Sciences, Central China Normal University, Wuhan, P.R.China.
Xuehui LiuNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, P.R.China.
David H DyerDepartment of Biochemistry and Entomology, College of Agricultural and Life Sciences, University of Wisconsin-Madison, Madison, United States of America.
Pingyong XuNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, P.R.China.
Kaiyu LiuSchool of Life Sciences, Central China Normal University, Wuhan, P.R.China.
Que LanDepartment of Biochemistry and Entomology, College of Agricultural and Life Sciences, University of Wisconsin-Madison, Madison, United States of America.
Huazhu HongSchool of Life Sciences, Wuhan Institute of Bioengineering, Wuhan, P.R.China.
Jianxin PengSchool of Life Sciences, Central China Normal University, Wuhan, P.R.China.
Rong PengSchool of Life Sciences, Central China Normal University, Wuhan, P.R.China.
Central China Normal University · CNUniversity of Wisconsin–Madison · USChinese Academy of Sciences · CNInstitute of Biophysics · CNWuhan Institute of Bioengineering · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cotton bollworm, Helicoverpa armigera, has developed strong resistance to many insecticides. Sterol Carrier Protein-2 (SCP-2) is an important non-specific lipid transfer protein in insects and appears to be a potential new target. In order to elucidate the structure and function of Helicoverpa armigera SCP-2 (HaSCP-2), NMR spectroscopy, docking simulations, mutagenesis and bioassays were performed. HaSCP-2 composed of five α-helices and four stranded β-sheets. The folds of α-helices and β-sheets interacted together to form a hydrophobic cavity with putative entrance and exit openings, which served as a tunnel for accommodating and transporting of lipids. Several sterols and fatty acids could interact with HaSCP-2 via important hydrophobic sites, which could be potential targets for insecticides. Mutagenesis experiments indicated Y51, F53, F89, F110, I117 and Q131 may be the key functional sites. HaSCP-2 showed high cholesterol binding activity and SCP-2 inhibitors (SCPIs) could inhibit the biological activity of HaSCP-2. SCPI-treated larvae at young stage showed a significant decrease of cholesterol uptake in vivo. Our study describes for the first time a NMR structure of SCP-2 in lepidopteran H. armigera and reveals its important function in cholesterol uptake, which facilitates the screening of effective insecticides targeting the insect cholesterol metabolism.

Indexed as

Models, MolecularNuclear Magnetic Resonance, BiomolecularProtein ConformationAmino Acid SequenceAnimalsCarrier ProteinsCholesterolGene ExpressionHydrophobic and Hydrophilic InteractionsInsecticidesLigandsMolecular Docking SimulationMolecular Dynamics SimulationMolecular Sequence DataMothsProtein BindingCarrier ProteinsCholesterolInsecticidesLigandsRecombinant Proteinssterol carrier proteins

Identifiers

PMID26655641
PMCPMC4674756
OpenAlexW2217327291

What OpenQuestion holds

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LicenceCC BY
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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.