Cited by 124Antibiotic Resistance in BacteriaAntibiotic Use and ResistancePharmaceutical and Antibiotic Environmental Impacts

Trends in β‐Lactam Resistance Among Enterobacteriaceae

Nordmann, Patrice·1998·Clinical Infectious Diseases

Abstract

beta-Lactam resistance among Enterobacteriaceae is related primarily to the emergence of novel beta-lactamases. The class A extended-spectrum beta-lactamases hydrolyze extended-spectrum beta-lactams and are inhibited by clavulanic acid. These beta-lactamases are divided in two groups: TEM and SHV derivatives and non-TEM and non-SHV extended-spectrum beta-lactamases (CTX-M1, CTX-M2, MEN-1, PER-1, PER-2, TOHO-1, and VEB-1). The plasmid-mediated cephalosporinases (MIR-1, FOX-1, MOX-1, BIL-1, CMY-1, CMY-2, and LAT-1) hydrolyze extended-spectrum cephalosporins and cephamycins and are not inhibited by clavulanic acid. They have been reported in Europe and in the United States. The 15 inhibitor-resistant penicillinases are TEM derivatives (except for SHV-10) and plasmid mediated, and they are mainly from Escherichia coli isolates. The carbapenemases noted among Enterobacteriaceae are either the chromosomally located penicillinases (Sme-1, NmcA, IMI-1) found in rare Enterobacter cloacae or Serratia marcescens isolates or the plasmid-mediated metalloenzyme IMP-1 that is widespread in Japan. The incidence of resistance among Enterobacteriaceae related to the other more common beta-lactam-resistance mechanisms has continued to rise worldwide.

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Crossref · 10.1086/514905

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  • Applying the β-lactam hierarchy to S pneumoniae is a stronger assumption than for Gram-negative bacteria because β-lactam resistance in Gram-negative bacteria is more commonly due to β-lactamases that often follow this hierarchy, whereas β-lactam resistance in S pneumoniae is often due to mutations in penicillin binding protein.

    “This is a stronger assumption for S pneumoniae than for the Gram-negative bacteria because the mechanism of resistance in Gram-negative bacteria is more commonly β-lactamases76 that often follow this hierarchy. By contrast, β-lactam resistance in S pneumoniae is often due to mutations77 in the penicillin binding protein”

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Authors
Nordmann, P.
Affiliations
Bicêtre Hospital (FR)
Corresponding author
Nordmann, Patrice
Venue
Clinical Infectious Diseases
Published
1998-08
Volume
27
Issue
s1
Pages
S100-S106
ISSN
  • 1058-4838 (ISSN-L)
  • 1537-6591
OpenAlex
W2005042941
Cited by
124
References
0
Citations by year
2026: 1 · 2025: 1 · 2024: 2 · 2023: 1 · 2022: 3 · 2021: 2 · 2019: 1 · 2018: 1 · 2017: 2 · 2016: 1 · 2015: 1 · 2014: 9 · 2013: 2 · 2012: 5
FWCI
5.52
Type
journal article
Language
en
Open access
closed
Locations
  • Clinical Infectious Diseases (publishedVersion)
  • PubMed (publishedVersion)
  • HighWire Press Open Archive (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Medicine › Antibiotic Resistance in Bacteria
  • Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Antibiotic Use and Resistance
  • Physical Sciences › Environmental Science › Pollution › Pharmaceutical and Antibiotic Environmental Impacts
Keywords
beta-lactam resistance, Enterobacteriaceae, extended-spectrum beta-lactamase, carbapenemase, IMP-1, Escherichia coli, Enterobacter cloacae, Serratia marcescens, clavulanic acid, CTX-M enzymes
MeSH terms
Animals, beta-Lactamases, Cephalosporinase, Enterobacteriaceae, Humans, Plasmids, Carbapenems, beta-Lactam Resistance, beta-Lactamase Inhibitors

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