Abstract
We developed a novel PCR method aimed at identi- fying and amplifying native codon sequences of muta- tion-prone amino acids in DNA gyrase implicated in quinolone resistance using a naturally occurring co- don bias in E. coli DNA gyrase A.
Highlights
The bacterial Deoxyribonucleic acid (DNA) gyrase enzyme induces negative supercoils in the DNA during replication and is the target of action for quinolone drugs [1]
We developed a novel PCR method aimed at identifying and amplifying native codon sequences of mutation-prone amino acids in DNA gyrase implicated in quinolone resistance using a naturally occurring codon bias in E. coli DNA gyrase A
The resistance patterns observed by disk diffusion method extrapolated on to the PAN PCR results that exhibited specific mutation patterns, except for one strain, which was resistant to quinolones in the disk diffusion method but did not exhibit any mutations in gyrase A (gyrA)
Summary
The bacterial DNA gyrase enzyme induces negative supercoils in the DNA during replication and is the target of action for quinolone drugs [1]. Escherichia coli ( E. coli) has 2 sub units, namely gyrase A (gyrA) and gyrase B (gyrB) that have molecular weights of 97 kDa and 90 kDa respectively [2]. GyrA interacts with DNA and cleaves it using its active site tyrosine residue (Tyr122) while GyrB has an ATPase active site. A small angle scattering X-ray study revealed the structure of GyrA and GyrB bound to DNA in E. coli [3]. Mutations in gyrase A (gyrA) lead to bacterial resistance to quinolone drugs. Substitution of serine at residue 83 (ser83) in gyrase A is the single most important reason for resistance to quinolones [4]. Mutations at ser of gyrA is the most frequent in Escherichia coli (E. coli) clinical isolates[5]. Mutation of ser to leucine (Leu) or tryptophan (Trp) confers high level resistance to quinolones while ser to Alanine (Ala) confers low level resi-
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