Mutations in Ribosomal Protein L3 Are Associated with Oxazolidinone Resistance in Staphylococci of Clinical Origin | Zendy

Jeffrey B. Locke | Zendy; M.T. Hilgers | Zendy; Karen Joy Shaw | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Mutations in Ribosomal Protein L3 Are Associated with Oxazolidinone Resistance in Staphylococci of Clinical Origin

Author(s) -

Jeffrey B. Locke,

M.T. Hilgers,

Karen Joy Shaw

Publication year - 2009

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.01032-09

Subject(s) - 23s ribosomal rna , linezolid , staphylococcus aureus , peptidyl transferase , ribosomal protein , staphylococcus epidermidis , ribosomal rna , biology , microbiology and biotechnology , staphylococcal infections , genetics , bacteria , ribosome , rna , gene , vancomycin

Following recent reports of ribosomal protein L3 mutations in laboratory-derived linezolid-resistant (LZD(r)) Staphylococcus aureus, we investigated whether similar mutations were present in LZD(r) staphylococci of clinical origin. Sequence analysis of a variety of LZD(r) isolates revealed two L3 mutations, DeltaSer145 (S. aureus NRS127) and Ala157Arg (Staphylococcus epidermidis 1653059), both occurring proximal to the oxazolidinone binding site in the peptidyl transferase center. The oxazolidinone torezolid maintained a >or=8-fold potency advantage over linezolid for both strains.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research