Contribution of natural amino acid substitutions in SHV extended-spectrum beta-lactamases to resistance against various beta-lactams.

ABSTRACT: SHV extended-spectrum beta-lactamases (ESBLs) arise through single amino acid substitutions in the parental enzyme, SHV-1. In order to evaluate the effect of genetic dissimilarities around the structural gene on MICs, we had previously devised an isogenic system of strains. Here, we present an extended version of the system that now allows assessment of all major types of SHV beta-lactamases as well as of two types of promoters of various strengths. Moreover, we devised a novel vector, pCCR9, to eliminate interference of the selection marker. A substitution within the signal sequence, I8F found in SHV-7, slightly increased MICs, suggesting more efficient transfer of enzyme precursor into the periplasmic space. We also noted that combination of G238S and E240K yielded higher resistance than

SUBMITTER: Randegger CC 

PROVIDER: S-EPMC90148 | biostudies-literature | 2000 Oct

REPOSITORIES: biostudies-literature