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Chapter 16 : Antimicrobial Resistance in Campylobacter

Authors: Jørgen Engberg1, Peter Gerner-Smidt2, Monika Keelan3, Diane E. Taylor4
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Affiliations: 1: Unit of Gastrointestinal Infections, Statens Serum Institut, Artillerivej 5, DK-2300 Copenhagen S, Denmark; 2: Unit of Gastrointestinal Infections, Statens Serum Institut, Artillerivej 5, DK-2300 Copenhagen S, Denmark; 3: Laboratory for Foodborne Zoonoses, Public Health Agency of Canada, and Department of Laboratory Medicine and Pathology, University of Alberta, Edmonton, Alberta T6G 2G3, Canada; 4: Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada
Content Type: Monograph
Publication Year: 2006

Category: Bacterial Pathogenesis

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Abstract:

This chapter provides a review of prevalence and trends of resistance in and isolated from humans in different parts of the world and a more thorough description of the mechanisms of resistance, origin, spread, and clinical consequences of resistance. Aminoglycosides exhibit rapid and significant bactericidal effects in vitro and should initially be included for the treatment of bacteremia in patients who appear very ill. The only mechanism of chloramphenicol resistance identified in occurs through modification of chloramphenicol by chloramphenicol acetyltransferase, which prevents its binding to the ribosome. The majority of contacts between Tet(O) and the ribosome are mediated by the rRNA, and one interaction with ribosomal protein S12. Most of the antimicrobials used in veterinary medicine are tetracyclines and macrolides, which result in high and continuous selective pressure for the animal-colonizing bacteria, ultimately resulting in the acquisition of antimicrobial resistance genes. Investigation into the mechanisms of action of antimicrobials, as well as the transfer of resistance determinants, is necessary to gain effective control of antimicrobial resistance. Epidemiological and microbiological studies show that poultry is the most important source for quinolone-susceptible and quinolone-resistant infections in humans. Trends over time for macrolide resistance show stable low rates in most countries, and macrolides should remain the drug class of choice for and enteritis.

Citation: Engberg J, Gerner-Smidt P, Keelan M, Taylor D. 2006. Antimicrobial Resistance in Campylobacter, p 269-292. In Aarestrup F (ed), Antimicrobial Resistance in Bacteria of Animal Origin. ASM Press, Washington, DC. doi: 10.1128/9781555817534.ch16

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Outer Membrane Proteins
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Antimicrobial Resistance in Campylobacter
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Citation: Engberg J, Gerner-Smidt P, Keelan M, Taylor D. 2006. Antimicrobial Resistance in Campylobacter, p 269-292. In Aarestrup F (ed), Antimicrobial Resistance in Bacteria of Animal Origin. ASM Press, Washington, DC. doi: 10.1128/9781555817534.ch16
/content/10.1128/9781555817534.chap16.fig16-1
Figure 1.

Trends for quinolone resistance rates (in percentages) among and combined from human sources around the world. The bars represent both nalidixic acid and fluoroquinolone resistance and are based on mean values of resistance from numerous reports. Updated and modified from reference . Additional data are from references , and , and V. Prouzet-Mauléon (personal communication).

10.1128/9781555817534/fig16-1_thmb.gif
10.1128/9781555817534/fig16-1.gif
Image of Figure 1.
Figure 1.

Trends for quinolone resistance rates (in percentages) among and combined from human sources around the world. The bars represent both nalidixic acid and fluoroquinolone resistance and are based on mean values of resistance from numerous reports. Updated and modified from reference . Additional data are from references , and , and V. Prouzet-Mauléon (personal communication).

Citation: Engberg J, Gerner-Smidt P, Keelan M, Taylor D. 2006. Antimicrobial Resistance in Campylobacter, p 269-292. In Aarestrup F (ed), Antimicrobial Resistance in Bacteria of Animal Origin. ASM Press, Washington, DC. doi: 10.1128/9781555817534.ch16
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Figure 2.

Quinolone resistance rates (in percentages) among (Denmark, The Netherlands, and Norway) and and combined (Finland, Sweden, the United Kingdom, and the United States) by history of travel. Data are from references , and .

10.1128/9781555817534/fig16-2_thmb.gif
10.1128/9781555817534/fig16-2.gif
Image of Figure 2.
Figure 2.

Quinolone resistance rates (in percentages) among (Denmark, The Netherlands, and Norway) and and combined (Finland, Sweden, the United Kingdom, and the United States) by history of travel. Data are from references , and .

Citation: Engberg J, Gerner-Smidt P, Keelan M, Taylor D. 2006. Antimicrobial Resistance in Campylobacter, p 269-292. In Aarestrup F (ed), Antimicrobial Resistance in Bacteria of Animal Origin. ASM Press, Washington, DC. doi: 10.1128/9781555817534.ch16
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Figure 3.

(A) Elongation cycle of protein synthesis; (B) inhibition by tetracycline (Tc); (C) model for Tet(O) action. (A) In the absence of antibiotics, the aa-tRNA–EF-Tu–GTP ternary complex catalyzes the binding of aa-tRNA to the open A site on the pretranslocation-state (Pre) ribosome. (B) Tc initially binds to the posttranslation-state (Post) ribosome and induces a conformational change (or steric clash) that blocks the aa-tRNA–EF-Tu–GTP ternary complex from occupying the A site, effectively inhibiting further protein synthesis. (C) If Tet(O) is present, it recognizes the Tc-blocked ribosome by virtue of its open A site, prolonged pausing, and possibly by a drug-induced conformational change. The interaction of Tet(O) with the ribosome induces rearrangements in the A site and triggers the release of Tc from the primary binding site prior to GTP hydrolysis. Tet(O) then hydrolyzes the bound GTP and likely leaves the ribosome with the GTPase-associated region in a configuration compatible with EF-Tu binding, thereby allowing protein synthesis to continue. Adapted from references and .

10.1128/9781555817534/fig16-3_thmb.gif
10.1128/9781555817534/fig16-3.gif
Image of Figure 3.
Figure 3.

(A) Elongation cycle of protein synthesis; (B) inhibition by tetracycline (Tc); (C) model for Tet(O) action. (A) In the absence of antibiotics, the aa-tRNA–EF-Tu–GTP ternary complex catalyzes the binding of aa-tRNA to the open A site on the pretranslocation-state (Pre) ribosome. (B) Tc initially binds to the posttranslation-state (Post) ribosome and induces a conformational change (or steric clash) that blocks the aa-tRNA–EF-Tu–GTP ternary complex from occupying the A site, effectively inhibiting further protein synthesis. (C) If Tet(O) is present, it recognizes the Tc-blocked ribosome by virtue of its open A site, prolonged pausing, and possibly by a drug-induced conformational change. The interaction of Tet(O) with the ribosome induces rearrangements in the A site and triggers the release of Tc from the primary binding site prior to GTP hydrolysis. Tet(O) then hydrolyzes the bound GTP and likely leaves the ribosome with the GTPase-associated region in a configuration compatible with EF-Tu binding, thereby allowing protein synthesis to continue. Adapted from references and .

Citation: Engberg J, Gerner-Smidt P, Keelan M, Taylor D. 2006. Antimicrobial Resistance in Campylobacter, p 269-292. In Aarestrup F (ed), Antimicrobial Resistance in Bacteria of Animal Origin. ASM Press, Washington, DC. doi: 10.1128/9781555817534.ch16
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Tables

Antimicrobial Resistance in Campylobacter
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Citation: Engberg J, Gerner-Smidt P, Keelan M, Taylor D. 2006. Antimicrobial Resistance in Campylobacter, p 269-292. In Aarestrup F (ed), Antimicrobial Resistance in Bacteria of Animal Origin. ASM Press, Washington, DC. doi: 10.1128/9781555817534.ch16
/content/10.1128/9781555817534.chap16.tab16-1
Table 1.

Erythromycin or azithromycin resistance rates among , , and and combined isolated from humans worldwide since 1997

Generic image for table
Table 1.

Erythromycin or azithromycin resistance rates among , , and and combined isolated from humans worldwide since 1997

Citation: Engberg J, Gerner-Smidt P, Keelan M, Taylor D. 2006. Antimicrobial Resistance in Campylobacter, p 269-292. In Aarestrup F (ed), Antimicrobial Resistance in Bacteria of Animal Origin. ASM Press, Washington, DC. doi: 10.1128/9781555817534.ch16
/content/10.1128/9781555817534.chap16.tab16-2
Table 2.

Antibiotics and their resistance mechanisms in Campylobacterspp.

Generic image for table
Table 2.

Antibiotics and their resistance mechanisms in Campylobacterspp.

Citation: Engberg J, Gerner-Smidt P, Keelan M, Taylor D. 2006. Antimicrobial Resistance in Campylobacter, p 269-292. In Aarestrup F (ed), Antimicrobial Resistance in Bacteria of Animal Origin. ASM Press, Washington, DC. doi: 10.1128/9781555817534.ch16
/content/10.1128/9781555817534.chap16.tab16-3
Table 3.

Antimicrobial agents transported by CmeABC in C. jejuni

Generic image for table
Table 3.

Antimicrobial agents transported by CmeABC in C. jejuni

Citation: Engberg J, Gerner-Smidt P, Keelan M, Taylor D. 2006. Antimicrobial Resistance in Campylobacter, p 269-292. In Aarestrup F (ed), Antimicrobial Resistance in Bacteria of Animal Origin. ASM Press, Washington, DC. doi: 10.1128/9781555817534.ch16
/content/10.1128/9781555817534.chap16.tab16-4
Table 4.

Studies evaluating the duration of illness in patients infected with quinolone-resistant strains versus quinolone-susceptible strains

Generic image for table
Table 4.

Studies evaluating the duration of illness in patients infected with quinolone-resistant strains versus quinolone-susceptible strains

Citation: Engberg J, Gerner-Smidt P, Keelan M, Taylor D. 2006. Antimicrobial Resistance in Campylobacter, p 269-292. In Aarestrup F (ed), Antimicrobial Resistance in Bacteria of Animal Origin. ASM Press, Washington, DC. doi: 10.1128/9781555817534.ch16
/content/10.1128/9781555817534.chap16.tab16-5
Table 5.

Campylobacter

Generic image for table
Table 5.

Campylobacter

Citation: Engberg J, Gerner-Smidt P, Keelan M, Taylor D. 2006. Antimicrobial Resistance in Campylobacter, p 269-292. In Aarestrup F (ed), Antimicrobial Resistance in Bacteria of Animal Origin. ASM Press, Washington, DC. doi: 10.1128/9781555817534.ch16

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