Evidence map›Paper›PMID 27552222›Full record

ArticlePloS one2016

A Diverse Family of Host-Defense Peptides (Piscidins) Exhibit Specialized Anti-Bacterial and Anti-Protozoal Activities in Fishes.

Scott A Salger, Katherine R Cassady, Benjamin J Reading, Edward J Noga

Abstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

  1. Review
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  3. Article
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  5. Article
  6. Article
  7. Infection of endemic chubParasitology · 2024
    Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Anti-Frontiers in microbiology · 2023
    Review
  14. Review
  15. Article
  16. Review
  17. Review
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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.

Scott A SalgerDepartment of Applied Ecology, North Carolina State University, Raleigh, North Carolina, United States of America.
Katherine R CassadyDepartment of Applied Ecology, North Carolina State University, Raleigh, North Carolina, United States of America.
Benjamin J ReadingDepartment of Applied Ecology, North Carolina State University, Raleigh, North Carolina, United States of America.
Edward J NogaDepartment of Clinical Sciences, North Carolina State University, College of Veterinary Medicine, Raleigh, North Carolina, United States of America.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Conventional antibiotics and other chemical-based drugs are currently one of the most common methods used to control disease-related mortality in animal agriculture. Use of the innate immune system to decrease disease related mortalities is a novel alternative to conventional drugs. One component of the innate immune system is the host-defense peptides, also known as antimicrobial peptides. Host-defense peptides are typically small, amphipathic, α-helical peptides with a broad-spectrum of action against viral, bacterial, fungal, and/or protozoal pathogens. Piscidins are host-defense peptides first discovered in the hybrid striped bass (white bass, Morone chrysops, x striped bass, M. saxatilis). In this paper we identify four new piscidin isoforms in the hybrid striped bass and describe their tissue distributions. We also determine the progenitor species of origin of each piscidin (orthology) and propose a revised nomenclature for this newly described piscidin family based on a three class system. The Class I piscidins (22 amino acids in length; striped bass and white bass piscidin 1 and piscidin 3) show broad-spectrum activity against bacteria and ciliated protozoans, while the Class III piscidins (55 amino acids in length; striped bass and white bass piscidin 6 and striped bass piscidin 7) primarily show anti-protozoal activity. The Class II piscidins (44-46 amino acids in length; striped bass and white bass piscidin 4 and white bass piscidin 5) have a level of activity against bacteria and protozoans intermediate to Classes I and III. Knowledge of piscidin function and activity may help in the future development of disease-resistant lines of striped bass and white bass that could be used to produce superior hybrids for aquaculture.

Indexed as

Immunity, InnateAmino Acid SequenceAnimalsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesDisease ResistanceFishesFish ProteinsGene ExpressionSequence AlignmentAnti-Bacterial AgentsAntimicrobial Cationic PeptidesFish Proteinsmoronecidin protein, Morone saxatilis

Identifiers

PMID27552222
PMCPMC4995043

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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.