Susceptibilities of beta-lactamase-positive and -negative strains of Campylobacter coli to beta-lactam agents

Abstract

The percentages of susceptibility of 28 strains of Campylobacter coli to 1-lactam agents were 96% for amoxicillin and ampicillin, 57% for ticarcillin, 4% for cefoxitin and cefuroxime, 61% for cefotaxime, and 11% for ceftazidime. None of the strains were susceptible to penicillin G, piperacillin, cefazolin, cephalothin, cefamandole, and cefoperazone. All strains were susceptible to imipenem and ciprofloxacin, and 21% were susceptible to erythromycin. A 13-lactamase was detected in 68% of the strains by cefinase disks and by the nitrocefin method. The 13-lactamase-positive strains were significantly less susceptible to amoxicillin, ampicillin, and ticarcillin than the 13-lactamase-negative strains (P < 0.003). Clavulanic acid (0.25 ,ug/ml) but not sulbactam and tazobactam (2 jg/ml) lowered to susceptible levels the amoxicillin and ampicillin MICs of the only strain of C. coli resistant to amoxicillin, ampicillin, and ticarcillin.Campylobacter coli has been recognized as a cause of human bacterial diarrhea and represents between 3 and 7% of Campylobacter human infections (1,8). Little is known about the ,B-lactam susceptibility pattern of C. coli. A few studies have reported data about ampicillin (4,12,14), amoxicillin (6, 14), cefotaxime (4, 6, 15), cephalothin (4, 10, 15), cefoperazone (14), and cefuroxime and penicillin G (15) susceptibility. ,B-Lactamase production was reported in 29 of 31 C coli tested by Fliegelman et al. (4). The purpose of this study was to determine the susceptibility pattern of C. coli to 3-lactam agents and to investigate the role of the ,-lactamase in the resistance to these antibiotics. The effect of clavulanic acid, sulbactam, and tazobactam on amoxicillin, ampicillin and ticarcillin was also studied.Ten strains of C. coli were obtained from a collection of 160 human thermophilic Campylobacter strains isolated in five hospitals in the Montreal area. Eighteen other human strains of C coli were obtained from the Laboratoire de Sante Publique du Quebec. Identification was done by the methods of the Centers for Disease Control, Atlanta, Ga. (8)

Antibiotic Resistance in Campylobacter Strains Isolated from Animals, Foods, and Humans in Spain in 1997–1998

“…Nevertheless, 206 Campylobacter strains were susceptible to ampicillin as determined by disk diffusion even though they were ␤-lactamase producers. Similar data were obtained by others (21,22,52). The ␤-lactamase-positive strains are significantly less susceptible to ampicillin even if the MICs detected in these strains are not high enough to be regarded as resistant (21,22).…”

“…A high level of erythromycin resistance was detected in C. jejuni strains isolated from foods of animal origin compared with the level obtained in strains from humans or broilers. Previous studies also observed low-level erythromycin resistance in C. jejuni isolated from humans or broilers (14,15,22,38,43). In our study, no erythromycin-resistant C. jejuni strains were found among those isolated from broilers.…”

Antimicrobial resistance of thermophilic Campylobacter

“…However, in some bacteria, changes in the penicillin-bindingproteins or lack of penetration of the drug into the bacteria are the main mechanisms of resistance. A large proportion of C. coli and C. jejuni produce beta-lactamases [29,30,50,62]. However, the β-lactamase of C. jejuni/coli seems to play a role only in resistance to amoxicillin, ampicillin and ticarcillin.…”

β-Lactamase-Mediated β-Lactam Resistance in Campylobacter Species: Prevalence of Cj0299 ( bla OXA-61 ) and Evidence for a Novel β-Lactamase in C . jejuni

“…The predominant ␤-lactamase found was termed type A, a 30-kDa protein with a pI of 8.3, which was active against penicillin, ampicillin, oxacillin, and carbenicillin and weakly active against cephalothin (cefalotin) but inactive against cephaloridine, cefuroxime, and cefotaxime. Lachance et al (12) showed that a ␤-lactamase from C. jejuni hydrolyzed ampicillin, amoxicillin, penicillin, and cloxacillin and partially hydrolyzed cephalothin. The profile of ␤-lactamase was similar to the profile of the type A enzyme reported by Lucain et al (14), had a pI of 8.8, and was inhibited by tazobactam, clavulanic acid, sulbactam, and cefoxitin but not EDTA or p-chloromercuribenzoate.…”