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JAC Advance Access originally published online on December 12, 2002
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Journal of Antimicrobial Chemotherapy (2003) 51, 157-161
© 2003 The British Society for Antimicrobial Chemotherapy

Comparative spectrum and activity of NVP-PDF386 (VRC4887), a new peptide deformylase inhibitor

Ronald N. Jones1,2 and Paul R. Rhomberg1,*

1 The JONES Group/JMI Laboratories, 345 Beaver Kreek Centre, Suite A, North Liberty, IA 52317; 2 Tufts University School of Medicine, Boston, MA, USA

Received 17 September 2002; returned 8 October 2002; revised 10 October 2002; accepted 22 October 2002

The antibacterial activity of NVP-PDF386 (VRC4887), a novel peptide deformylase (PDF) inhibitor, was tested against over 1000 recent clinical isolates collected during 2001 and 2002. The MIC50/90 (mg/L) results for NVP-PDF386 (VRC4887) were: Staphylococcus aureus (SA) 0.5/1, coagulase-negative staphylococci (CoNS) 0.5/1, Streptococcus pneumoniae 0.25/0.5, other streptococci 0.25/0.5, enterococci 1/2, Moraxella catarrhalis 0.25/0.25, Haemophilus influenzae 8/32 and Enterobacteriaceae or non-fermentative Gram-negative bacilli >32/>32 mg/L. No differences in NVP-PDF386/(VRC4887) MIC distributions were observed between methicillin-resistant (MR) S. aureus and methicillin-susceptible (MS) S. aureus, MR-CoNS and MS-CoNS, penicillin-susceptible and non-susceptible streptococci, and macrolide-susceptible and -resistant strains. The potency of NVP-PDF386 (VRC4887) compared favourably with those of control compounds, including glycopeptides, oxazolidinones, a streptogramin combination and other agents with activity focused against Gram-positive cocci.

Keywords: antimicrobial activity, peptide deformylase inhibitor, NVP-PDF386

* Corresponding author. Tel: +1-319-665-3370; Fax: +1-319-665-3371; E-mail: paul-rhomberg{at}jmilabs.com


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