This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Wise, R.
Right arrow Articles by Ashby, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wise, R.
Right arrow Articles by Ashby, J.

 Previous Article  |  Next Article 

Antimicrobial Agents and Chemotherapy, April 2002, p. 1117-1118, Vol. 46, No. 4
0066-4804/02/$04.00+0     DOI: 10.1128/AAC.46.4.1117-1118.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

In Vitro Activities of Peptide Deformylase Inhibitors against Gram-Positive Pathogens

R. Wise,* J. M. Andrews, and J. Ashby

Department of Microbiology, City Hospital NHS Trust, Birmingham, United Kingdom

Received 14 May 2001/ Returned for modification 25 November 2001/ Accepted 3 January 2002

The activities of six peptide deformylase (PDF) inhibitors against 107 respiratory tract pathogens were studied and compared to those of ciprofloxacin and amoxicillin-clavulanate. Against Streptococcus pneumoniae, BB-83698 and BB-83815 were the most active PDF inhibitors (MIC at which 90% of the organisms tested were inhibited [MIC90], 0.25 µg/ml). Five of the agents showed similar activity against Moraxella catarrhalis (MIC90, 0.12 µg/ml). All PDF inhibitors were less active against Haemophilus influenzae; BB-3497 was the most active agent (MIC90, 2 µg/ml). Five agents were studied against Chlamydia spp. and showed activity similar to that of ciprofloxacin (MIC, 0.5 to 4 µg/ml). This study demonstrates that PDF inhibitors have the potential to be developed for the treatment of respiratory tract infections.

* Corresponding author. Mailing address: Department of Microbiology, City Hospital NHS Trust, Birmingham, United Kingdom. Phone: 44 121 507 4255. Fax: 44 121 551 7763. E-mail: r.wise{at}bham.ac.uk.

Antimicrobial Agents and Chemotherapy, April 2002, p. 1117-1118, Vol. 46, No. 4
0066-4804/02/$04.00+0     DOI: 10.1128/AAC.46.4.1117-1118.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Dean, C. R., Narayan, S., Daigle, D. M., Dzink-Fox, J. L., Puyang, X., Bracken, K. R., Dean, K. E., Weidmann, B., Yuan, Z., Jain, R., Ryder, N. S. (2005). Role of the AcrAB-TolC Efflux Pump in Determining Susceptibility of Haemophilus influenzae to the Novel Peptide Deformylase Inhibitor LBM415. Antimicrob. Agents Chemother. 49: 3129-3135 [Abstract] [Full Text]  
  • Fritsche, T. R., Sader, H. S., Cleeland, R., Jones, R. N. (2005). Comparative Antimicrobial Characterization of LBM415 (NVP PDF-713), a New Peptide Deformylase Inhibitor of Clinical Importance. Antimicrob. Agents Chemother. 49: 1468-1476 [Abstract] [Full Text]  
  • Ramanathan-Girish, S., McColm, J., Clements, J. M., Taupin, P., Barrowcliffe, S., Hevizi, J., Safrin, S., Moore, C., Patou, G., Moser, H., Gadd, A., Hoch, U., Jiang, V., Lofland, D., Johnson, K. W. (2004). Pharmacokinetics in Animals and Humans of a First-in-Class Peptide Deformylase Inhibitor. Antimicrob. Agents Chemother. 48: 4835-4842 [Abstract] [Full Text]  
  • Lofland, D., Difuntorum, S., Waller, A., Clements, J. M., Weaver, M. K., Karlowsky, J. A., Johnson, K. (2004). In vitro antibacterial activity of the peptide deformylase inhibitor BB-83698. J Antimicrob Chemother 53: 664-668 [Abstract] [Full Text]  
  • Gross, M., Clements, J., Beckett, R. P., Thomas, W., Taylor, S., Lofland, D., Ramanathan-Girish, S., Garcia, M., Difuntorum, S., Hoch, U., Chen, H., Johnson, K. W. (2004). Oral anti-pneumococcal activity and pharmacokinetic profiling of a novel peptide deformylase inhibitor. J Antimicrob Chemother 53: 487-493 [Abstract] [Full Text]  
  • Cynamon, M. H., Alvirez-Freites, E., Yeo, A. E. T. (2004). BB-3497, a peptide deformylase inhibitor, is active against Mycobacterium tuberculosis. J Antimicrob Chemother 53: 403-405 [Full Text]  
  • Azoulay-Dupuis, E., Mohler, J., Bedos, J. P. (2004). Efficacy of BB-83698, a Novel Peptide Deformylase Inhibitor, in a Mouse Model of Pneumococcal Pneumonia. Antimicrob. Agents Chemother. 48: 80-85 [Abstract] [Full Text]  
  • Roblin, P. M., Hammerschlag, M. R. (2003). In Vitro Activity of a New Antibiotic, NVP-PDF386 (VRC4887), against Chlamydia pneumoniae. Antimicrob. Agents Chemother. 47: 1447-1448 [Abstract] [Full Text]  
  • Jones, R. N., Rhomberg, P. R. (2003). Comparative spectrum and activity of NVP-PDF386 (VRC4887), a new peptide deformylase inhibitor. J Antimicrob Chemother 51: 157-161 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»