Evidence map›Paper›PMID 22438972›Full record

ArticlePloS one2012

Evaluation of an antimicrobial L-amino acid oxidase and peptide derivatives from Bothropoides mattogrosensis pitviper venom.

Brunna M Okubo, Osmar N Silva, Ludovico Migliolo, Diego G Gomes, William F Porto, Carla L Batista, Carmel S Ramos, Hortência H S Holanda, Simoni C Dias, Octavio L Franco and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

19 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
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  3. Article
  4. Review
  5. Review
  6. Article
  7. P-I metalloproteinases and L-amino acid oxidases fromThe journal of venomous animals and toxins including tropical diseases · 2021
    Article
  8. Article
  9. Article
  10. Antimicrobial Activity of Protein Fraction fromMolecules (Basel, Switzerland) · 2020
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Snake venom L-amino acid oxidases: an overview on their antitumor effects.The journal of venomous animals and toxins including tropical diseases · 2014
    Review
  16. Review
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  18. 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

11 authors at 2 institutions in 1 country.

Brunna M OkuboPrograma de Pós-Graduação em Biotecnologia, Universidade Católica Dom Bosco, Campo Grande, Mato Grosso do Sul, Brazil.
Osmar N Silva
Ludovico Migliolo
Diego G Gomes
William F Porto
Carla L Batista
Carmel S Ramos
Hortência H S Holanda
Simoni C Dias
Octavio L Franco
Susana E Moreno
Universidade Católica Dom Bosco · BRUniversidade Federal de Juiz de Fora · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Healthcare-associated infections (HAIs) are causes of mortality and morbidity worldwide. The prevalence of bacterial resistance to common antibiotics has increased in recent years, highlighting the need to develop novel alternatives for controlling these pathogens. Pitviper venoms are composed of a multifaceted mixture of peptides, proteins and inorganic components. L-amino oxidase (LAO) is a multifunctional enzyme that is able to develop different activities including antibacterial activity. In this study a novel LAO from Bothrops mattogrosensis (BmLAO) was isolated and biochemically characterized. Partial enzyme sequence showed full identity to Bothrops pauloensis LAO. Moreover, LAO here isolated showed remarkable antibacterial activity against Gram-positive and -negative bacteria, clearly suggesting a secondary protective function. Otherwise, no cytotoxic activities against macrophages and erythrocytes were observed. Finally, some LAO fragments (BmLAO-f1, BmLAO-f2 and BmLAO-f3) were synthesized and further evaluated, also showing enhanced antimicrobial activity. Peptide fragments, which are the key residues involved in antimicrobial activity, were also structurally studied by using theoretical models. The fragments reported here may be promising candidates in the rational design of new antibiotics that could be used to control resistant microorganisms.

Indexed as

Amino Acid SequenceAnimalsAntimicrobial Cationic PeptidesCrotalid VenomsDrug Evaluation, PreclinicalGram-Negative BacteriaGram-Positive BacteriaHumansIn Vitro TechniquesL-Amino Acid OxidaseMicrobial Sensitivity TestsModels, MolecularMolecular Sequence DataPeptide FragmentsProtein ConformationSequence Homology, Amino AcidAntimicrobial Cationic PeptidesCrotalid VenomsL-Amino Acid OxidasePeptide Fragments

Identifiers

PMID22438972
PMCPMC3306279
OpenAlexW2034604903

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.