Skip Navigation

This Article
Right arrow Full Text (PDF)
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 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 arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Livemore, D. M.
Right arrow Articles by Leung, Y. K
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Livemore, D. M.
Right arrow Articles by Leung, Y. K
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Journal of Antimicrobial Chemotherapy (1987) 20, 313-321
© 1987 The British Society for Antimicrobial Chemotherapy


research-article

ß-Lactamase of Pseudomonas pseudomallei and its contribution to antibiotic resistance

D. M. Livemorea,*, P. Y. Chau, Alice I. W. Wong and Y. K Leung

Department of Microbiology, University of Hong Kong Pokfulam Road, Hong Kong aDepartment of Medical Microbiology, The London Hospital Medical College Turner Street, London El 2AD, UK

Received 10 March 1987;


*Corresponding author

ß-Lactamase production was examined in nine strains of Pseudomonas pseudomallei isolated from human, animal and environmental sources in Thailand and Hong Kong. All produced the same weakly inducible, membrane associated chromosomal cephalosporinase, which had a molecular weight of 29,500 and an isoelectric point of 7.4–7.7. The enzyme resembled the cefuroximases ofPs. cepaciaandProteus vulgaris, but differed from the Class I cephalosporinases typical of Ps. aeruginosa and most enterobacteria, in being strongly active against carbenicillin, cefotaxime and cefuroxime and in being inactivated readily by clavulanic acid. Synergy experiments with clavulanic acid investigated the enzyme's contribution to antibiotic resistance, and these results broadly correlated with those of in-vitro hydrolysis assays. Thus, ampicillin, carbenicillin, cefoperazone, cefotaxime, cefuroxime and cephalothin, which were hydrolysed in vitro, were potentiated four to 64-fold by 2 mg/l clavulanic acid; but cefoxitin, ceftazidime, cloxacillin and imipenem, which appeared stable in vitro, were potentiated four-fold or less.


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
Clin. Microbiol. Rev.Home page
A. C. Cheng and B. J. Currie
Melioidosis: Epidemiology, Pathophysiology, and Management
Clin. Microbiol. Rev., April 1, 2005; 18(2): 383 - 416.
[Abstract] [Full Text] [PDF]


Home page
Antimicrob. Agents Chemother.Home page
C. Tribuddharat, R. A. Moore, P. Baker, and D. E. Woods
Burkholderia pseudomallei Class A {beta}-Lactamase Mutations That Confer Selective Resistance against Ceftazidime or Clavulanic Acid Inhibition
Antimicrob. Agents Chemother., July 1, 2003; 47(7): 2082 - 2087.
[Abstract] [Full Text] [PDF]


Home page
Antimicrob. Agents Chemother.Home page
A.-S. Morin, L. Poirel, F. Mory, R. Labia, and P. Nordmann
Biochemical-Genetic Analysis and Distribution of DES-1, an Ambler Class A Extended-Spectrum {beta}-Lactamase from Desulfovibrio desulfuricans
Antimicrob. Agents Chemother., October 1, 2002; 46(10): 3215 - 3222.
[Abstract] [Full Text] [PDF]


Home page
J Antimicrob ChemotherHome page
P. Niumsup and V. Wuthiekanun
Cloning of the class D {beta}-lactamase gene from Burkholderia pseudomallei and studies on its expression in ceftazidime-susceptible and -resistant strains
J. Antimicrob. Chemother., October 1, 2002; 50(4): 445 - 455.
[Abstract] [Full Text] [PDF]


Home page
Antimicrob. Agents Chemother.Home page
T. K. M. Cheung, P. L. Ho, P. C. Y. Woo, K. Y. Yuen, and P. Y. Chau
Cloning and Expression of Class A {beta}-Lactamase Gene blaABPS in Burkholderia pseudomallei
Antimicrob. Agents Chemother., April 1, 2002; 46(4): 1132 - 1135.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
H. J. Bootsma, P. C. Aerts, G. Posthuma, T. Harmsen, J. Verhoef, H. van Dijk, and F. R. Mooi
Moraxella (Branhamella) catarrhalis BRO beta -Lactamase: a Lipoprotein of Gram-Positive Origin?
J. Bacteriol., August 15, 1999; 181(16): 5090 - 5093.
[Abstract] [Full Text]


Home page
J Antimicrob ChemotherHome page
M. Afzal-Shah, H. E. Villar, and D. M. Livermore
Biochemical characteristics of a carbapenemase from an Acinetobacter baumannii isolate collected in Buenos Aires, Argentina
J. Antimicrob. Chemother., January 1, 1999; 43(1): 127 - 131.
[Abstract] [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.