Evidence map›Paper›PMID 21554953›Full record

ArticleInsect biochemistry and molecular biology2011

Antiviral, anti-parasitic, and cytotoxic effects of 5,6-dihydroxyindole (DHI), a reactive compound generated by phenoloxidase during insect immune response.

Picheng Zhao, Zhiqiang Lu, Michael R Strand, Haobo Jiang

Open access · greenAbstract read
In one paragraph

Article in Insect biochemistry and molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

48 citing papers in PubMed, 113 citations in OpenAlex.

  1. Article
  2. Article
  3. Frontiers in veterinary science · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
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  10. Review
  11. Article
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  14. Article
  15. Why do insects evolve immune priming? A search for crossroads.Developmental and comparative immunology · 2022
    Review
  16. Article
  17. Review
  18. Article
  19. Article
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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

4 authors at 2 institutions in 1 country.

Picheng ZhaoDepartment of Entomology and Plant Pathology, Oklahoma State University, 127 NRC, Stillwater, OK 74078, USA.
Zhiqiang Lu
Michael R Strand
Haobo Jiang
Oklahoma State University · USUniversity of Georgia · US

Funding

Initiation and Regulation of Prophenoloxidase ActivationR01GM058634 · NIGMS · OKLAHOMA STATE UNIVERSITY STILLWATER · PI JIANG, HAOBO · 1999 to 2022
$4.0M
NIGMS NIH HHS GM58634NIGMS NIH HHS R01 GM058634
6 · The paper itself

Abstract

Phenoloxidase (PO) and its activation system are implicated in several defense responses of insects. Upon wounding or infection, inactive prophenoloxidase (proPO) is converted to active PO through a cascade of serine proteases and their homologs. PO generates reactive compounds such as 5,6-dihydroxyindole (DHI), which have a broad-spectrum antibacterial and antifungal activity. Here we report that DHI and its spontaneous oxidation products are also active against viruses and parasitic wasps. Preincubation of a baculovirus stock with 1.25 mM DHI for 3 h near fully disabled recombinant protein production. The LC₅₀ for lambda bacteriophage and eggs of the wasp Microplitis demolitor were 5.6 ± 2.2 and 111.0 ± 1.6 μM, respectively. The toxicity of DHI and related compounds also extended to cells derived from insects that serve as hosts for several of the aforementioned pathogens. Pretreatment of Sf9 cells with 1.0 mM DHI for 4 h resulted in 97% mortality, and LC₅₀ values of 20.3 ± 1.2 μM in buffer and 131.8 ± 1.1 μM in a culture medium. Symptoms of DHI toxicity in Sf9 cells included DNA polymerization, protein crosslinking, and lysis. Taken together, these data showed that proPO activation and DHI production is strongly toxic against various pathogens but can also damage host tissues and cells if not properly controlled.

Indexed as

AnimalsBacteriophage lambdaCell LineCytotoxicity, ImmunologicDNAEnzyme ActivationIndolesInsect ProteinsKineticsMonophenol MonooxygenaseNucleopolyhedrovirusesOxidation-ReductionPolymerizationRecombinant ProteinsSpodopteraSubstrate Specificity5,6-dihydroxyindoleDNAIndolesInsect ProteinsMonophenol MonooxygenaseRecombinant Proteins

Identifiers

PMID21554953
PMCPMC3129360
OpenAlexW2063875317

What OpenQuestion holds

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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.