Evidence map›Paper›PMID 22267667›Full record

ArticleApplied and environmental microbiology2012

Enhanced staphylolytic activity of the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88 HydH5 virion-associated peptidoglycan hydrolase: fusions, deletions, and synergy with LysH5.

Lorena Rodríguez-Rubio, Beatriz Martínez, Ana Rodríguez, David M Donovan, Pilar García

Open access · bronzeAbstract readEvaluation Study
In one paragraph

Article in Applied and environmental microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

51 citing papers in PubMed, 80 citations in OpenAlex.

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  13. Gut Microbiome Proteomics in Food Allergies.International journal of molecular sciences · 2023
    Review
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  15. Article
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  18. PeerJ · 2022
    Article
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  20. Antimicrobial Peptides: An Update on Classifications and Databases.International journal of molecular sciences · 2021
    Review
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 at 2 institutions in 2 countries.

Lorena Rodríguez-RubioInstituto de Productos Lácteos de Asturias (IPLA-CSIC), Asturias, Spain.
Beatriz Martínez
Ana Rodríguez
David M Donovan
Pilar García
Instituto de Productos Lácteos de Asturias · ESUnited States Department of Agriculture · US

Funding

Triple action chimera: eradication of nasal S. aureus by cell wall hydrolasesR01AI075077 · NIAID · U.S. AGRICULTURAL RESEARCH CENTER · PI DONOVAN, DAVID MATTHEW · 2008 to 2010
$697k
NIAID NIH HHS 1R01AI075077-01A1NIAID NIH HHS R01 AI075077
6 · The paper itself

Abstract

Virion-associated peptidoglycan hydrolases have potential as antimicrobial agents due to their ability to lyse Gram-positive bacteria on contact. In this work, our aim was to improve the lytic activity of HydH5, a virion-associated peptidoglycan hydrolase from the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88. Full-length HydH5 and two truncated derivatives containing only the CHAP (cysteine, histidine-dependent amidohydrolase/peptidase) domain exhibited high lytic activity against live S. aureus cells. In addition, three different fusion proteins were created between lysostaphin and HydH5, each of which showed higher staphylolytic activity than the parental enzyme or its deletion construct. Both parental and fusion proteins lysed S. aureus cells in zymograms and plate lysis and turbidity reduction assays. In plate lysis assays, HydH5 and its derivative fusions lysed bovine and human S. aureus strains, the methicillin-resistant S. aureus (MRSA) strain N315, and human Staphylococcus epidermidis strains. Several nonstaphylococcal bacteria were not affected. HydH5 and its derivative fusion proteins displayed antimicrobial synergy with the endolysin LysH5 in vitro, suggesting that the two enzymes have distinct cut sites and, thus, may be more efficient in combination for the elimination of staphylococcal infections.

Indexed as

BacteriolysisStaphylococcus PhagesAnimalsAnti-Bacterial AgentsCattleCattle DiseasesDrug SynergismEndopeptidasesGene DeletionHumansMethicillin-Resistant Staphylococcus aureusMolecular Sequence DataN-Acetylmuramoyl-L-alanine AmidaseRecombinant Fusion ProteinsStaphylococcal InfectionsStaphylococcus aureusAnti-Bacterial AgentsendolysinEndopeptidasesN-Acetylmuramoyl-L-alanine AmidaseRecombinant Fusion Proteins

Identifiers

PMID22267667
PMCPMC3302612
OpenAlexW4233298540

What OpenQuestion holds

Textmetadata
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.