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Chapter 22 : Enterococcus

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Enterococcus, Page 1 of 2

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Abstract:

is the species most frequently isolated in humans, accounting for 80 to 90% of enterococcal isolates, whereas represents between 5 and 10% of clinical isolates. Nearly 15 other enterococcal species may be occasionally associated with infections, including , , , , and . The lower MIC breakpoint of vancomycin (4 mg/liter) divides the bacterial population, with certain isolates being categorized as susceptible. In and , two types of mechanisms account for increased resistance to the penicillins. Enterococci can acquire resistance to aminoglycosides by three mechanisms: modification of the ribosomal target, alteration of antibiotic transport, and enzymic modification of the drugs. Oxazolidinones bind to the ribosomal peptidyltransferase center, domain V of 23S rRNA, and prevent formation of the initiation complex formed by -formyl-methionyl-tRNA, ribosomes, mRNA, and initiation factors IF2 and IF3, therefore blocking protein synthesis at an early stage. In a large number of isolates, resistance is due to diacetylation of an hydroxyl group of the molecule by chloramphenicol-acetyltransferases (CAT) encoded by genes. Similar genes are found in enterococci, streptococci, and staphylococci, confirming active exchange of resistance determinants between these species. The antiseptic resistance gene , originally isolated from gram-negative bacteria, was found by Japanese authors in 9 of 48 strains of clinical isolates of .

Citation: Leclercq R, Courvalin P. 2005. Enterococcus, p 299-313. In White D, Alekshun M, McDermott P (ed), Frontiers in Antimicrobial Resistance. ASM Press, Washington, DC. doi: 10.1128/9781555817572.ch22

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Mobile Genetic Elements
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Major Facilitator Superfamily
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First Generation Quinolones
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Third Generation Cephalosporins
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Tables

Generic image for table
Table 1

Intrinsic resistance in enterococci

Citation: Leclercq R, Courvalin P. 2005. Enterococcus, p 299-313. In White D, Alekshun M, McDermott P (ed), Frontiers in Antimicrobial Resistance. ASM Press, Washington, DC. doi: 10.1128/9781555817572.ch22
Generic image for table
Table 2

Aminoglycoside-modifying enzymes in enterococci

AMI, amikacin; BUT, butirosin; FOR, fortimicin; GENC1, gentamicin C1; KAN, kanamycin; ISE, isepamycin; KM, kanamycin; LIV, lividomycin; NEO, neomycin; NET, netilmicin; RIB, ribostamycin; SIS, sisomicin; SPE, spectinomycin; STR, streptomycin; TOB, tobramycin.

Part of the bifunctional enzyme AAC(6′)-APH(2″).

Intrinsic resistance in .

Citation: Leclercq R, Courvalin P. 2005. Enterococcus, p 299-313. In White D, Alekshun M, McDermott P (ed), Frontiers in Antimicrobial Resistance. ASM Press, Washington, DC. doi: 10.1128/9781555817572.ch22
Generic image for table
Table 3

Macrolide-lincosamide-streptogramin resistance genes in enterococci

MLS, macrolides-lincosamides-streptogramins B; M, 14-, 15-membered-ring macrolides; MS, macrolides-streptogramins B; L, lincosamides; LS, lincosamides-streptogramins A; S, streptogramins A-type; S, streptogramins B type.

Citation: Leclercq R, Courvalin P. 2005. Enterococcus, p 299-313. In White D, Alekshun M, McDermott P (ed), Frontiers in Antimicrobial Resistance. ASM Press, Washington, DC. doi: 10.1128/9781555817572.ch22

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