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Antimicrobial Agents and Chemotherapy, July 2005, p. 2625-2633, Vol. 49, No. 7
0066-4804/05/$08.00+0     doi:10.1128/AAC.49.7.2625-2633.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Putative VanRS-Like Two-Component Regulatory System Associated with the Inducible Glycopeptide Resistance Cluster of Paenibacillus popilliae

Henry Fraimow,1* Christopher Knob,1 Inmaculada A. Herrero,2,{dagger} and Robin Patel2

Division of Infectious Diseases, Cooper Health System and University of Medicine and Dentistry of New Jersey, 401 Haddon Avenue, Room 274, Camden, New Jersey 08103,1 Division of Infectious Diseases, Mayo Clinic College of Medicine, 200 First Street Southwest, Rochester, Minnesota 559052

Received 17 November 2004/ Returned for modification 17 December 2004/ Accepted 26 February 2005

Paenibacillus popilliae contains vanF encoding a putative D-Ala:D-lactate (D-Lac) ligase, VanF, as part of the vanYFZFHFFXF cluster that is similar in structure to the enterococcal vanA and vanB clusters. Using growth curves, we demonstrated that vancomycin resistance in P. popilliae is inducible. Using degenerate oligonucleotides targeted at bacterial cell wall ligases, we identified a second ligase gene with features of a D-Ala:D-Ala ligase in both P. popilliae and the related, vancomycin-susceptible, Paenibacillus lentimorbus. The 3,380-bp region upstream of vanYFZFHFFXF in P. popilliae ATCC 14706 was sequenced and found to contain genes encoding a putative two-component regulator, VanRFSF, similar to VanRS but more closely related to a family of two-component regulators linked to VanY-like carboxypeptidases in several glycopeptide-susceptible Bacillus species. This upstream region also included a transposase similar to a transposase found in Bacillus halodurans and, in some strains, a 99-bp insertion of unknown function with 95% nucleotide identity to a portion of the Tn1546 transposase gene. Analysis of glycopeptide resistance-associated clusters from soil and/or insect-dwelling organisms may provide important clues to the molecular evolution of acquired glycopeptide resistance elements in human pathogens.


* Corresponding author. Mailing address: Division of Infectious Diseases, Cooper University Hospital, 401 Haddon Ave., Room 274, Camden, NJ 08103. Phone: (856) 757-7767. Fax: (856) 757-7803. E-mail: fraimow-henry{at}cooperhealth.edu.

{dagger} Present address: Sanidad Animal Facultad de Veterinaria (UCM), Av. Puerta de Hierro s/n, Madrid, Spain 28040.


Antimicrobial Agents and Chemotherapy, July 2005, p. 2625-2633, Vol. 49, No. 7
0066-4804/05/$08.00+0     doi:10.1128/AAC.49.7.2625-2633.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.




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