Evidence map›Paper›PMID 23567591›Full record

ArticleInsect biochemistry and molecular biology2013

Gloverins of the silkworm Bombyx mori: structural and binding properties and activities.

Hui-Yu Yi, Xiao-Juan Deng, Wan-Ying Yang, Cong-Zhao Zhou, Yang Cao, Xiao-Qiang Yu

Open access · greenAbstract read
In one paragraph

Article in Insect biochemistry and molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

15 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Diversity of Antimicrobial Peptides in Silkworm.Life (Basel, Switzerland) · 2023
    Review
  3. Article
  4. Article
  5. Microbiology (Reading, England) · 2020
    Article
  6. Article
  7. Antimicrobial peptides fromRSC advances · 2019
    Review
  8. Article
  9. Antibacterial Mechanism of Gloverin2 from Silkworm,International journal of molecular sciences · 2018
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Insect antimicrobial peptides and their applications.Applied microbiology and biotechnology · 2014
    Review
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.

Hui-Yu YiLaboratory of Insect Molecular Biology and Biotechnology, Guangdong Provincial Key Laboratory of Agro-animal Genomics and Molecular Breeding, College of Animal Science, South China Agricultural University, Guangzhou 510642, China.
Xiao-Juan Deng
Wan-Ying Yang
Cong-Zhao Zhou
Yang Cao
Xiao-Qiang Yu
South China Agricultural University · CNUniversity of Missouri–Kansas City · USUniversity of Science and Technology of China · CN

Funding

Lectins in Insect ImmunityR01GM066356 · NIGMS · UNIVERSITY OF MISSOURI KANSAS CITY · PI YU, XIAO-QIANG · 2002 to 2011
$1.9M
NIGMS NIH HHS GM066356NIGMS NIH HHS R01 GM066356
6 · The paper itself

Abstract

Gloverins are basic, glycine-rich and heat-stable antibacterial proteins (∼14- kDa) in lepidopteran insects with activity against Escherichia coli, Gram-positive bacteria, fungi and a virus. Hyalophora gloveri gloverin adopts a random coil structure in aqueous solution but has α-helical structure in membrane-like environment, and it may interact with the lipid A moiety of lipopolysaccharide (LPS). Manduca sexta gloverin binds to the O-specific antigen and outer core carbohydrate of LPS. In the silkworm Bombyx mori, there are four gloverins with slightly acidic to neutral isoelectric points. In this study, we investigate structural and binding properties and activities of B. mori gloverins (BmGlvs), as well as correlations between structure, binding property and activity. Recombinant BmGlv1-4 were expressed in bacteria and purified. Circular dichroism (CD) spectra showed that all four BmGlvs mainly adopted random coli structure (>50%) in aqueous solution in regardless of pH, but contained α-helical structure in the presence of 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP), smooth and rough mutants (Ra, Rc and Re) of LPS and lipid A. Plate ELISA assay showed that BmGlvs at pH 5.0 bound to rough mutants of LPS and lipid A but not to smooth LPS. Antibacterial activity assay showed that positively charged BmGlvs (at pH 5.0) were active against E. coli mutant strains containing rough LPS but inactive against E. coli with smooth LPS. Our results suggest that binding to rough LPS is the prerequisite for the activity of BmGlvs against E. coli.

Indexed as

Amino Acid SequenceAnimalsAnti-Bacterial AgentsBombyxCircular DichroismEscherichia coliInsect ProteinsIntercellular Signaling Peptides and ProteinsLipopolysaccharidesProtein BindingProteinsProtein Structure, SecondaryAnti-Bacterial AgentsgloverinInsect ProteinsIntercellular Signaling Peptides and ProteinsLipopolysaccharidesProteins

Identifiers

PMID23567591
PMCPMC3760519
OpenAlexW2080269881

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.