Skip Navigation


JAC Advance Access originally published online on January 6, 2003
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
51/2/247    most recent
dkg036v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (6)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Yoshida, R.
Right arrow Articles by Hiramatsu, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yoshida, R.
Right arrow Articles by Hiramatsu, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?


Journal of Antimicrobial Chemotherapy (2003) 51, 247-255
© 2003 The British Society for Antimicrobial Chemotherapy

Physiological and molecular analysis of a mecA-negative Staphylococcus aureus clinical strain that expresses heterogeneous methicillin resistance

Reiko Yoshida1, Kyoko Kuwahara-Arai1, Tadashi Baba1, Longzhu Cui1, Judith F. Richardson2 and Keiichi Hiramatsu1,*

1 Department of Bacteriology, Juntendo University, 2-1-1 Hongo, Bunkyo-ku, Tokyo 113, Japan; 2 Central Public Health Laboratory, London, UK

Received 24 January 2002; returned 22 July 2002; revised 5 September 2002; accepted 14 October 2002

Staphylococcus aureus clinical isolate 61/5896 exhibited methicillin resistance (MIC 64 mg/L), but lacked mecA, which encodes penicillin-binding protein 2'. The strain was isolated in England in 1961, and exhibited unstable heterogeneous methicillin resistance. When cultivated in drug-free medium, the methicillin resistance of 61/5896 increased after three daily passages, then decreased and was completely lost after 12 days’ passage. Electron microscopy revealed that strain 61/5896 had a thicker and rougher cell wall than its methicillin-susceptible derivatives. It produced about three times more penicillin-binding protein 2 (PBP2) than methicillin-susceptible derivatives. The strain was characteristically a non-producer of autolytic enzyme, though the phenotype, which was lost easily, was not directly correlated with methicillin resistance.

Keywords: PBP2, PBP2', mecA, MRSA, autolysis

* Corresponding author. Tel: +81-3-5802-1040; Fax: +81-3-5684-7830; E-mail: hiram{at}juntendo.ac.jp


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J Med MicrobiolHome page
J. Nadarajah, M. J. S. Lee, L. Louie, L. Jacob, A. E. Simor, M. Louie, and M. J. McGavin
Identification of different clonal complexes and diverse amino acid substitutions in penicillin-binding protein 2 (PBP2) associated with borderline oxacillin resistance in Canadian Staphylococcus aureus isolates.
J. Med. Microbiol., December 1, 2006; 55(Pt 12): 1675 - 1683.
[Abstract] [Full Text] [PDF]

Home page
 J. Clin. Microbiol.Home page
A. L. d. C. Darini, I. C. V. Palazzo, and A. Felten
Cefoxitin Does Not Induce Production of Penicillin Binding Protein 2a in Methicillin-Susceptible Staphylococcus aureus Strains
J. Clin. Microbiol., September 1, 2004; 42(9): 4412 - 4413.
[Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.