Evidence map›Paper›PMID 26976231›Full record

ArticleDevelopmental and comparative immunology2016

Characterization and regulation of expression of an antifungal peptide from hemolymph of an insect, Manduca sexta.

Qasim Al Souhail, Yasuaki Hiromasa, Mohammad Rahnamaeian, Martha C Giraldo, Daisuke Takahashi, Barbara Valent, Andreas Vilcinskas, Michael R Kanost

Abstract read
In one paragraph

Article in Developmental and comparative immunology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 35 citations in OpenAlex.

  1. Insect Antimicrobial Peptides as Guardians of Immunity and Beyond: A Review.International journal of molecular sciences · 2024
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. His-Ala-Phe-Lys peptide fromFrontiers in microbiology · 2022
    Article
  8. Article
  9. Article
  10. Identification and recombinant expression of an antimicrobial peptide (cecropin B-like) from soybean pestThe journal of venomous animals and toxins including tropical diseases · 2021
    Article
  11. Article
  12. Tobacco Hornworm (Virulence · 2020
    Article
  13. Mosquito-fungus interactions and antifungal immunity.Insect biochemistry and molecular biology · 2019
    Review
  14. Article
  15. Recent Advances in the Use ofJournal of fungi (Basel, Switzerland) · 2018
    Review
  16. Article
  17. Article
  18. Article
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

8 authors at 2 institutions in 2 countries.

Qasim Al SouhailDepartment of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS 66506, USA.
Yasuaki HiromasaDepartment of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS 66506, USA.
Mohammad RahnamaeianLOEWE Center for Insect Biotechnology and Bioresources, Fraunhofer Institute for Molecular Biology and Applied Ecology (IME), Giessen Winchesterstrasse 2, 35394 Giessen, Germany.
Martha C GiraldoDepartment of Plant Pathology, Kansas State University, Manhattan, KS 66506, USA.
Daisuke TakahashiDepartment of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS 66506, USA.
Barbara ValentDepartment of Plant Pathology, Kansas State University, Manhattan, KS 66506, USA.
Andreas VilcinskasLOEWE Center for Insect Biotechnology and Bioresources, Fraunhofer Institute for Molecular Biology and Applied Ecology (IME), Giessen Winchesterstrasse 2, 35394 Giessen, Germany; Institute for Insect Biotechnology, Justus-Liebig-University of Giessen, Heinrich-Buff-Ring 26-32, 39592 Giessen, Germany.
Michael R KanostDepartment of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS 66506, USA. Electronic address: kanost@ksu.edu.
Kansas State University · USFraunhofer Institute for Molecular Biology and Applied Ecology · DE

Funding

Supplement 2 to promote diversity in health related res.: protease systems in insR37GM041247 · NIGMS · KANSAS STATE UNIVERSITY · PI KANOST, MICHAEL R · 2011 to 2020
$3.8M
SERINE PROTEINASE INHIBITORS IN INSECTSR01GM041247 · NIGMS · KANSAS STATE UNIVERSITY · PI KANOST, MICHAEL R · 1994 to 2010
$3.1M
NIGMS NIH HHS R01 GM041247NIGMS NIH HHS R37 GM041247
6 · The paper itself

Abstract

Insects secrete antimicrobial peptides as part of the innate immune response. Most antimicrobial peptides from insects have antibacterial but not antifungal activity. We have characterized an antifungal peptide, diapausin-1 from hemolymph of a lepidopteran insect, Manduca sexta (tobacco hornworm). Diapausin-1 was isolated by size exclusion chromatography from hemolymph plasma of larvae that were previously injected with a yeast, Saccharomyces cerevisiae. Fractions containing activity against S. cerevisiae were analyzed by SDS-PAGE and MALDI-TOF MS/MS and found to contain a 45-residue peptide that was encoded by sequences identified in M. sexta transcriptome and genome databases. A cDNA for diapausin-1 was cloned from cDNA prepared from fat body RNA. Diapausin-1 is a member of the diapausin family of peptides, which includes members known to have antifungal activity. The M. sexta genome contains 14 genes with high similarity to diapausin-1, each with 6 conserved Cys residues. Diapausin-1 was produced as a recombinant protein in Escherichia coli. Purified recombinant diapausin-1 was active against S. cerevisiae, with IC50 of 12 μM, but had no detectable activity against bacteria. Spores of some plant fungal pathogens treated with diapausin-1 had curled germination tubes or reduced and branched hyphal growth. Diapausin-1 mRNA level in fat body strongly increased after larvae were injected with yeast or with Micrococcus luteus. In addition, diapausin-1 mRNA levels increased in midgut and fat body at the wandering larval stage prior to pupation, suggesting developmental regulation of the gene. Our results indicate that synthesis of diapausin-1 is part of an antifungal innate immune response to infection in M. sexta.

Indexed as

AnimalsAntifungal AgentsAntigens, FungalCloning, MolecularFat BodyGene Expression Regulation, DevelopmentalGram-Positive Bacterial InfectionsHemolymphInsect ProteinsLarvaManducaMass SpectrometryMicrococcus luteusPeptidesSaccharomyces cerevisiaeAntifungal AgentsAntigens, FungalInsect ProteinsPeptidesAntifungalHemolymphImmunityInsectYeast

Identifiers

PMID26976231
PMCPMC4866881
OpenAlexW2302391529

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.