SHV-27, a novel cefotaxime-hydrolysing β-lactamase, identified in Klebsiella pneumoniae isolates from a Brazilian hospital

• Published in: Journal of antimicrobial chemotherapy 2001-04, Vol.47 (4), p.463-465
• Main Authors: Corkill, John E., Cuevas, Luis E., Gurgel, Ricardo Q., Greensill, Julie, Hart, C. Anthony
• Format: Article
• Language: English
• Subjects: Anti-Bacterial Agents - metabolism; Anti-Bacterial Agents - pharmacology; Antibacterial agents; Antibiotics. Antiinfectious agents. Antiparasitic agents; Aztreonam - pharmacology; Bacteriology; beta-Lactamases - isolation & purification; beta-Lactamases - metabolism; Biological and medical sciences; Brazil; Cefotaxime - metabolism; Cefotaxime - pharmacology; Ceftazidime - pharmacology; DNA Mutational Analysis; Drug Resistance, Microbial - genetics; Electrophoresis, Gel, Pulsed-Field; Fundamental and applied biological sciences. Psychology; Genetics; Hospitals; Humans; Klebsiella pneumoniae - drug effects; Klebsiella pneumoniae - enzymology; Klebsiella pneumoniae - genetics; Klebsiella pneumoniae - isolation & purification; Medical sciences; Microbial Sensitivity Tests; Microbiology; Molecular Sequence Data; Pharmacology. Drug treatments; Point Mutation - genetics; Polymorphism, Restriction Fragment Length
• ISSN: 0305-7453; 1460-2091; 1460-2091
• DOI: 10.1093/jac/47.4.463

From a collection of cefotaxime-resistant Klebsiella pneumoniae isolated from neonatal blood culture specimens in a maternity hospital in Aracaju, Brazil, two isolates (strains KPBRZ-842 and -843, indistinguishable by pulsed-field gel electrophoresis) were found to produce β-lactamases with isoelectric points (pI) of 5.4 and 8.2, respectively. Using a gel overlay method, cefotaxime hydrolysis was shown to be associated with the pI 8.2 protein. Nucleotide sequencing of the gene encoding the pI 8.2 β-lactamase revealed a blaSHV-ESBL-type gene differing from the gene encoding SHV-1 by three silent point mutations, and a fourth that resulted in an amino acid substitution, aspartate for glycine, at position 156. This novel SHV-type extended-spectrum β-lactamase is designated SHV-27.