Evidence map›Paper›PMID 22484285›Full record

ArticlePeptides2012

Lysine substitutions convert a bacterial-agglutinating peptide into a bactericidal peptide that retains anti-lipopolysaccharide activity and low hemolytic activity.

Mahsa Abdolhosseini, Seshagiri R Nandula, Jonathan Song, Helmut Hirt, Sven-Ulrik Gorr

Abstract read
In one paragraph

Article in Peptides, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Efficacy of gigantol, a bibenzyl compound, againstJournal of oral microbiology · 2025
    Article
  9. Frankincense (Current issues in molecular biology · 2024
    Article
  10. Article
  11. Article
  12. Peptides in Dentistry: A Scoping Review.Bioengineering (Basel, Switzerland) · 2023
    Article
  13. Review
  14. Article
  15. Interactions of two enantiomers of a designer antimicrobial peptide with structural components of the bacterial cell envelope.Journal of peptide science : an official publication of the European Peptide Society · 2022
    Article
  16. Article
  17. Antimicrobial and enzyme-responsive multi-peptide surfaces for bone-anchored devices.Materials science & engineering. C, Materials for biological applications · 2021
    Article
  18. Article
  19. Article
  20. 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

5 authors.

Mahsa AbdolhosseiniDepartment of Diagnostic and Biological Sciences, University of Minnesota School of Dentistry, Minneapolis, MN 55455, USA. abd_mahsa@yahoo.com
Seshagiri R Nandula
Jonathan Song
Helmut Hirt
Sven-Ulrik Gorr

Funding

Antibacterial and anti-inflammatory activities of Parotid Secretory ProteinR01DE017989 · NIDCR · UNIVERSITY OF MINNESOTA · PI GORR, SVEN-ULRIK · 2010 to 2013
$1.4M
NIDCR NIH HHS R01 DE017989NIDCR NIH HHS R01DE17989
6 · The paper itself

Abstract

GL13NH2 is a bacteria-agglutinating peptide derived from the sequence of the salivary protein parotid secretory protein (PSP, BPIFA2, SPLUNC2, C20orf70). The peptide agglutinates both Gram negative and Gram positive bacteria, and shows anti-lipopolysaccharide activity in vitro and in vivo. However, GL13NH2 does not exhibit bactericidal activity. To generate a more cationic peptide with potential bactericidal activity, three amino acid residues were replaced with lysine residues to generate the peptide GL13K. In this report, the antibacterial and anti-inflammatory activities of GL13K were characterized. GL13K had lost the ability to agglutinate bacteria but gained bactericidal activity. Substitution of individual amino acids in GL13K with alanine did not restore bacterial agglutination. GL13K was bactericidal against Pseudomonas aeruginosa, Streptococcus gordonii and Escherichia coli but not Porphyromonas gingivalis. Unlike the agglutinating activity of GL13NH2, the bactericidal activity of GL13K against P. aeruginosa was retained in the presence of saliva. Both GL13NH2 and GL13K exhibited anti-lipopolysaccharide activity. In GL13K, this activity appeared to depend on a serine hydroxyl group. GL13K protected mice from lipopolysaccharide-induced sepsis and the peptide exhibited a low level of hemolysis, suggesting that it may be suitable for in vivo application.

Indexed as

Antimicrobial Cationic PeptidesAgglutinationAmino Acid SubstitutionAnimalsAnti-Bacterial AgentsAnti-Infective AgentsEscherichia coliHemolysisLipopolysaccharidesLysineMaleMiceMice, Inbred C57BLPeptide FragmentsPorphyromonas gingivalisPseudomonas aeruginosaAnti-Bacterial AgentsAnti-Infective AgentsAntimicrobial Cationic PeptidesLipopolysaccharidesLysinePeptide Fragments

Identifiers

PMID22484285
PMCPMC3356437

What OpenQuestion holds

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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.