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Antimicrobial Agents and Chemotherapy, October 2005, p. 4227-4233, Vol. 49, No. 10
0066-4804/05/$08.00+0 doi:10.1128/AAC.49.10.4227-4233.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Unité des Agents Antibactériens, Institut Pasteur, Paris,1 Institut de Biochimie et de Biophysique Moléculaire et Cellulaire, Université Paris-Sud, Orsay, France2
Received 17 May 2005/ Returned for modification 28 June 2005/ Accepted 23 July 2005
The sequence and gene organization of the van operons in vancomycin (MIC of >256 µg/ml)- and teicoplanin (MIC of
32 µg/ml)-resistant Paenibacillus thiaminolyticus PT-2B1 and Paenibacillus apiarius PA-B2B isolated from soil were determined. Both operons had regulatory (vanR and vanS), resistance (vanH, vanA, and vanX), and accessory (vanY, vanZ, and vanW) genes homologous to the corresponding genes in enterococcal vanA and vanB operons. The vanAPT operon in P. thiaminolyticus PT-2B1 had the same gene organization as that of vanA operons whereas vanAPA in P. apiarius PA-B2B resembled vanB operons due to the presence of vanW upstream from the vanHAX cluster but was closer to vanA operons in sequence. Reference P. apiarius strains NRRL B-4299 and NRRL B-4188 were found to harbor operons indistinguishable from vanAPA by PCR mapping, restriction fragment length polymorphism, and partial sequencing, suggesting that this operon was species specific. As in enterococci, resistance was inducible by glycopeptides and associated with the synthesis of pentadepsipeptide peptidoglycan precursors ending in D-Ala-D-Lac, as demonstrated by D,D-dipeptidase activities, high-pressure liquid chromatography, and mass spectrometry. The precursors differed from those in enterococci by the presence of diaminopimelic acid instead of lysine in the peptide chain. Altogether, the results are compatible with the notion that van operons in soil Paenibacillus strains and in enterococci have evolved from a common ancestor.
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