ArticleAntimicrobial agents and chemotherapy2006
Proteomic study of peptide deformylase inhibition in Streptococcus pneumoniae and Staphylococcus aureus.
Article in Antimicrobial agents and chemotherapy, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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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.
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Who cites it
5 citing papers in PubMed, 11 citations in OpenAlex.
- Aureolib - a proteome signature library: towards an understanding of staphylococcus aureus pathophysiology.PloS one · 2013Article
- Solvent-assisted slow conversion of a dithiazole derivative produces a competitive inhibitor of peptide deformylase.Biochimica et biophysica acta · 2010Article
- The ORFeome of Staphylococcus aureus v 1.1.BMC genomics · 2008Article
- Drug forecast - the peptide deformylase inhibitors as antibacterial agents.Therapeutics and clinical risk management · 2007Article
- Formyl-methionine as a degradation signal at the N-termini of bacterial proteins.Microbial cell (Graz, Austria)Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peptide deformylase (PDF) is an essential enzyme in both gram-negative and gram-positive bacteria. It hydrolyzes formylated N-terminal peptides to generate free N-terminal peptides during the process of protein maturation. Inhibition of this enzyme results in cessation of bacterial growth. We have examined the effect of a potent PDF inhibitor, LBM-415 (also known as VIC-104959), on the proteomes of Staphylococcus aureus and Streptococcus pneumoniae using two-dimensional electrophoresis. Both S. aureus and S. pneumoniae showed accumulation of many N-terminal formylated peptides/proteins upon PDF inhibition. In S. pneumoniae, formylated peptide/protein accumulation was time dependent. Following inhibition, subsequent removal of the inhibitor resulted in deformylation of formylated peptides/proteins; this recovery process was also time dependent. If instead the inhibited cells were maintained in the presence of sub-MIC levels of the PDF inhibitor, the formylated peptides/proteins remained for a much longer time, which correlated with a prolonged postantibiotic effect in vitro. These observations may have broader implications for the application of this class of antibiotics in vivo.
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