![]() According to mutation profiles of their ftsI, strains were classified as group I ( n = 3), group II ( n = 4), group–III–like ( n = 1) and group III ( n = 1). Our isolates belonged mainly to biotype IV and I and were non-typeable and genetically unrelated. One strain from each group was resistant to cefotaxime. Biotyping and clonality were performed by API-NH and pulsed-field gel electrophoresis, respectively.įour strains were β-lactamase-negative ampicillin-resistant and five were β-lactamase-positive clavulanic-acid-resistant. This study aimed to characterize the polymorphism of ftsI gene in 19 H. influenzae strains, isolated between 20 (different resistance phenotypes to β-lactams ( n = 9) and susceptible strains ( n = 10) used for comparative purposes).Īll strains were characterized for capsular type by PCR and agglutination tests and for β-lactam resistance by amplification and sequencing of ftsI. The decreased affinity to β-lactams in Haemophilus influenzae is usually caused by specific alterations in penicillin-binding protein 3 due to varieties of substitutions in ftsI gene.
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