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J Med Microbiol 56 (2007), 236-240; DOI: 10.1099/jmm.0.46778-0
© 2007 Society for General Microbiology
ISSN 1473-5644

Polymorphisms of the pbp5 gene and correlation with ampicillin resistance in Enterococcus faecium isolates of animal origin

Patricia Poeta1,2,3, Daniela Costa1,2, Gilberto Igrejas4, Yolanda Sáenz2, Myriam Zarazaga2, Jorge Rodrigues1,3 and Carmen Torres2

1 Departamento de Ciências Veterinárias, Universidade de Trás-os-Montes e Alto Douro, Vila Real, Portugal

2 Área de Bioquímica y Biología Molecular, Universidad de La Rioja, Logroño, Spain

3 Centro de Estudos de Ciências Animais e Veterinárias, Vila Real, Portugal

4 Departamento de Genética e Biotecnologia, Universidade de Trás-os-Montes e Alto Douro, Vila Real, Portugal

Correspondence
Carmen Torres
carmen.torres{at}daa.unirioja.es

Received 12 June 2006
Accepted 5 October 2006

The C-terminal region of the pbp5 gene was sequenced in 11 ampicillin-resistant and 5 ampicillin-susceptible Enterococcus faecium isolates of animal origin, and compared with a pbp5 reference sequence (GenBank accession no. X84860). Eight different pbp5 alleles (designated A–H) were detected when amino acid changes in the region 461–629 were considered. Three of these alleles (A–C) were detected in ampicillin-susceptible isolates (MIC range 1–8 µg ml–1), and included the changes 470H->Q, 471V->I, 487Q->L, 581I->V, 595E->A or 622E->D. The remaining five alleles (D–H) were found in ampicillin-resistant isolates (MIC range 32–256 µg ml–1); three of these alleles (F–H) presented a serine insertion at position 466', in addition to other important amino acid changes (485M->A, 496N->K, 499A->T, 525E->D, 586V->L or 629E->V). The other two alleles presented the amino acid changes 496N->K and 629E->V (allele D), and 470H->Q (allele F). A correlation between deduced amino acid changes in PBP5 and ampicillin MICs was detected in animal E. faecium isolates.

Abbreviations: PBP5, penicillin-binding protein 5.






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