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Journal of Bacteriology, January 2008, p. 508-514, Vol. 190, No. 2
0021-9193/08/$08.00+0     doi:10.1128/JB.01549-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Penicillin-Binding Proteins and Cell Wall Composition in β-Lactam-Sensitive and -Resistant Strains of Staphylococcus sciuri{triangledown}

Yanjiao Zhou,1,2,{dagger} Aude Antignac,1,{dagger} Shang Wei Wu,1,2 and Alexander Tomasz1*

Laboratory of Microbiology, The Rockefeller University, New York, New York 10021,1 Department of Microbiology, Tianjin Medical University, Tianjin, People's Republic of China2

Received 26 September 2007/ Accepted 7 November 2007

A close homologue of the acquired Staphylococcus aureus mecA gene is present as a native gene in Staphylococcus sciuri. We determined the patterns of penicillin-binding proteins (PBPs) and the peptidoglycan compositions of several S. sciuri strains to explore the functions of this mecA homologue, named pbpD, in its native S. sciuri environment. The protein product of pbpD was identified as PBP4 with a molecular mass of 84 kDa, one of the six PBPs present in representatives of each of three subspecies of S. sciuri examined. PBP4 had a low affinity for nafcillin, reacted with a monoclonal antibody raised against S. aureus PBP2A, and was greatly overproduced in oxacillin-resistant clinical isolate S. sciuri SS37 and to a lesser extent in resistant laboratory mutant K1M200. An additional PBP inducible by oxacillin and corresponding to S. aureus PBP2A was identified in another oxacillin-resistant clinical isolate, S. sciuri K3, which harbors an S. aureus copy of mecA. Oxacillin resistance depended on the overtranscribed S. sciuri pbpD gene in strains SS37 and K1M200, while the resistance of strain K3 depended on the S. aureus copy of mecA. Our data provide evidence that both S. aureus mecA and S. sciuri pbpD can function as resistance determinants in either an S. aureus or an S. sciuri background and that the protein products of these genes, S. aureus PBP2A and S. sciuri PBP4, can participate in the biosynthesis of peptidoglycan, the muropeptide composition of which depends on the bacterium "hosting" the resistance gene.


* Corresponding author. Mailing address: Laboratory of Microbiology, The Rockefeller University, 1230 York Avenue, New York, NY 10021. Phone: (212) 327-8277. Fax: (212) 327-8688. E-mail: tomasz{at}rockefeller.edu

{triangledown} Published ahead of print on 16 November 2007.

{dagger} Y.Z and A.A. contributed equally to this work.


Journal of Bacteriology, January 2008, p. 508-514, Vol. 190, No. 2
0021-9193/08/$08.00+0     doi:10.1128/JB.01549-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.







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