Prevalence of OmpK35 and OmpK36 porin expression in beta-lactamase and non-betalactamase- producing Klebsiella pneumoniae.

Autor:	Shakib P; Clinical Microbiology Research Center, Ilam University of Medical Sciences, Ilam., Ghafourian S, Zolfaghary MR, Hushmandfar R, Ranjbar R, Sadeghifard N
Jazyk:	angličtina
Zdroj:	Biologics : targets & therapy [Biologics] 2012; Vol. 6, pp. 1-4. Date of Electronic Publication: 2011 Dec 22.
DOI:	10.2147/BTT.S27582
Abstrakt:	Background: The aims of this study were to confirm the presence of OmpK35 and OmpK36 in extended-spectrum beta-lactamase-producing and nonextended-spectrum beta-lactamase-producing Klebsiella pneumoniae and to determine the relationship between porin expression and resistance to third-generation cephalosporins. Methods: Fifty-two K. pneumoniae isolates were obtained and analyzed for extended-spectrum beta-lactamase and for OmpK35 and OmpK36. Results: Twenty-two (42.3%) isolates of K. pneumoniae were extended-spectrum beta-lactamase producers. The OmpK35 profile in K. pneumoniae producing extended-spectrum beta-lactamase showed the presence of porin protein in ceftazidime-sensitive K. pneumoniae (six isolates), and the OmpK36 profile in K. pneumoniae producing extended-spectrum beta-lactamase revealed isolates sensitive to cefotaxime (n = 8) and ceftriaxone (n = 6). All nonextended-spectrum beta-lactamase-producing K. pneumoniae showed the presence of OmpK35 and OmpK36 porin proteins. Conclusion: The presence of OmpK35 is mostly related to ceftazidime susceptibility and less to cefotaxime and ceftriaxone susceptibility, while OmpK36 expression is seen more often in cefotaxime-sensitive isolates. OmpK35 and OmpK36 indicate nonextended-spectrum beta-lactamase producing strains, and their presence is important when selecting an antimicrobial agent.
Databáze:	MEDLINE
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