Comparison of basal media for culturing Campylobacter jejuni and Campylobacter coli

Ng, L.-K.; Stiles, Michael E.; Taylor, Diane E.

doi:10.1128/jcm.21.2.226-230.1985

Cited by 21 publications

(7 citation statements)

References 22 publications

(22 reference statements)

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“…jejuni grows best in microaerobic environments (i.e., 5 to 10% oxygen, 3 to 10% carbon dioxide) (22) at 42°C. It will grow on a variety of basal media including brucella and Mueller-Hinton agars (127). However, optimal isolation from routine specimens requires the addition of selective (57) and nutritional supplements.…”

Section: Introductionmentioning

confidence: 99%

Pathophysiology of Campylobacter enteritis.

Walker¹,

Caldwell²,

Lee³

et al. 1986

Microbiological Reviews

189

112

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Section: Introductionmentioning

confidence: 99%

Pathophysiology of Campylobacter enteritis.

Walker¹,

Caldwell²,

Lee³

et al. 1986

Microbiological Reviews

189

112

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“…Although many types of media can be used to culture C. jejuni , Mueler-Hinton is reported to have the highest recovery rate. 44 Culture media and agar plates (solid media) were warmed to 42 °C before each use.…”

Section: Methodsmentioning

confidence: 99%

Transition-State Analogues of Campylobacter jejuni 5′-Methylthioadenosine Nucleosidase

et al. 2018

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Campylobacter jejuni is a Gram-negative bacterium responsible for food-borne gastroenteritis and associated with Guillain-Barré, Reiter, and irritable bowel syndromes. Antibiotic resistance in C. jejuni is common, creating a need for antibiotics with novel mechanisms of action. Menaquinone biosynthesis in C. jejuni uses the rare futalosine pathway, where 5′-methylthioadenosine nucleosidase (CjMTAN) is proposed to catalyze the essential hydrolysis of adenine from 6-amino-6-deoxyfutalosine to form dehypoxanthinylfutalosine, a menaquinone precursor. The substrate specificity of CjMTAN is demonstrated to include 6-amino-6-deoxyfutalosine, 5′-methylthioadenosine, S-adenosylhomocysteine, adenosine, and 5′-deoxyadenosine. These activities span the catalytic specificities for the role of bacterial MTANs in menaquinone synthesis, quorum sensing, and S-adenosylmethionine recycling. We determined inhibition constants for potential transition-state analogues of CjMTAN. The best of these compounds have picomolar dissociation constants and were slow-onset tight-binding inhibitors. The most potent CjMTAN transition-state analogue inhibitors inhibited C. jejuni growth in culture at low micromolar concentrations, similar to gentamicin. The crystal structure of apoenzyme C. jejuni MTAN was solved at 1.25 Å, and five CjMTAN complexes with transition-state analogues were solved at 1.42 to 1.95 Å resolution. Inhibitor binding induces a loop movement to create a closed catalytic site with Asp196 and Ile152 providing purine leaving group activation and Arg192 and Glu12 activating the water nucleophile. With inhibitors bound, the interactions of the 4′-alkylthio or 4′-alkyl groups of this inhibitor family differ from the Escherichia coli MTAN structure by altered protein interactions near the hydrophobic pocket that stabilizes 4′-substituents of transition-state analogues. These CjMTAN inhibitors have potential as specific antibiotic candidates against C. jejuni.

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“…Morphology was established using phase contrast microscopy and Gram's staining, while phenotypic profiling was assessed using the biochemical tests oxidase, catalase, indoxyl acetate hydrolysis, hippuricase activity, H 2 S production in ferric bisulphite pyruvate (FBP) media, DNase activity, H 2 S production in TSI media, urease activity, and nitrate reduction [3,11–15]. Growth was assayed on MH agar containing 10% sheep blood at 25°C, 37°C, and 42°C, while growth tolerance was carried out in aliquots of modified Brucella broth [16], each supplemented with 1% glycine, 1% bile, and 3.5% NaCl. Disc diffusion was used to evaluate the antimicrobial susceptibility of organisms to nalidixic acid (30 μg), cephalothin (30 μg), and polymyxin B (300 IU) (Becton Dickinson, Cockeysville, MD).…”

Section: Methodsmentioning

confidence: 99%

Differentiation of Clinical Helicobacter pullorum Isolates from Related Helicobacter and Campylobacter Species

Melito¹,

Woodward²,

Bernard

et al. 2000

Helicobacter

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Phenotypic and genotypic procedures were used to identify H. pullorum. Interspecies phenotypic variability was apparent and supported the use of a polyphasic approach for identification. Similarities to the more prominent human pathogens Campylobacter coli and C. lari were also noted. The use of a combination of phenotypic and, in particular, genotypic markers for H. pullorum should prove valuable both for epidemiological investigations and for the diagnosis of disease related to this emerging human pathogen.

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Comparison of basal media for culturing Campylobacter jejuni and Campylobacter coli

Abstract: agar base (Oxoid); Columbia blood agar base supplemented with 10% defibrinated sheep blood, with 1.5 or 3% agar; and Mueller-Hinton agar (Difco). Inoculated plates were incubated at 37°C in a 7% C02 atmosphere and counted after 48 and 72 h of incubation.

Cited by 21 publications

References 22 publications

Pathophysiology of Campylobacter enteritis.

Pathophysiology of Campylobacter enteritis.

Transition-State Analogues of Campylobacter jejuni 5′-Methylthioadenosine Nucleosidase

Differentiation of Clinical Helicobacter pullorum Isolates from Related Helicobacter and Campylobacter Species

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