Β-lactam resistance: Difference between revisions
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Β-lactam resistance
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*Porin channel mutations that reduce antibiotic influx |
*Porin channel mutations that reduce antibiotic influx |
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| − | ==β-lactamases== |
+ | ===β-lactamases=== |
| − | * |
+ | *Also see [[Β-lactamases]] |
| − | ===Ambler Classification of ß-lactamases=== |
+ | ====Ambler Classification of ß-lactamases==== |
*Based on amino acid sequences rather than function |
*Based on amino acid sequences rather than function |
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{| class="wikitable" |
{| class="wikitable" |
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| + | !Class |
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| − | !Ambler |
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!Binding Site |
!Binding Site |
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!Examples |
!Examples |
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| − | ===Specific ß-lactamases=== |
+ | ====Specific ß-lactamases==== |
*TEM-1: most common β-lactamase in Gram-negative bacteria |
*TEM-1: most common β-lactamase in Gram-negative bacteria |
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*KPC: most common carbapenemase |
*KPC: most common carbapenemase |
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*NDM-1: broad-spectrum metallo-β-lactamase and carbapenemase |
*NDM-1: broad-spectrum metallo-β-lactamase and carbapenemase |
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| − | *OXA-48: most common carbapenemase in [[Acinetobacter |
+ | *OXA-48: most common carbapenemase in [[Acinetobacter]] |
| − | ==Efflux Pumps== |
+ | ===Efflux Pumps=== |
*Major cause of resistance in [[Pseudomonas aeruginosa]] and similar species |
*Major cause of resistance in [[Pseudomonas aeruginosa]] and similar species |
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*e.g. MexAB-OprM, which confers broad antimicrobial resistance including cephalosporins and some carbapanems |
*e.g. MexAB-OprM, which confers broad antimicrobial resistance including cephalosporins and some carbapanems |
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| − | ==Porin Loss== |
+ | ===Porin Loss=== |
*Most common cause of carbapenem resistance in [[Pseudomonas aeruginosa]] |
*Most common cause of carbapenem resistance in [[Pseudomonas aeruginosa]] |
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| + | == Management == |
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| + | * See also [[Carbapenem-resistant organisms]] |
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[[Category:Antibiotics]] |
[[Category:Antibiotics]] |
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Latest revision as of 12:10, 2 April 2022
Mechanisms
- ß-lactamase production: enzymatic breakdown of beta lactam antibiotic
- Penicillin binding protein mutations (e.g. MRSA)
- Efflux pump mutations
- Porin channel mutations that reduce antibiotic influx
β-lactamases
- Also see β-lactamases
Ambler Classification of ß-lactamases
- Based on amino acid sequences rather than function
- Classes A, C, and D are serine ß-lactamases, while class B are metallo-β-lactamases
| Class | Binding Site | Examples | Inhibitors |
|---|---|---|---|
| A | serine | TEM, SHV, KPC, CTX-M, GES | avibactam, vaborbactam, relebactam |
| B | metallo | VIM, NDM, IMP | |
| C | serine | AmpC, P99 | avibactam, vaborbactam, relebactam |
| D | serine | OXA (oxacillinase) enzymes | avibactam (OXA-48) |
Specific ß-lactamases
- TEM-1: most common β-lactamase in Gram-negative bacteria
- KPC: most common carbapenemase
- NDM-1: broad-spectrum metallo-β-lactamase and carbapenemase
- OXA-48: most common carbapenemase in Acinetobacter
Efflux Pumps
- Major cause of resistance in Pseudomonas aeruginosa and similar species
- e.g. MexAB-OprM, which confers broad antimicrobial resistance including cephalosporins and some carbapanems
Porin Loss
- Most common cause of carbapenem resistance in Pseudomonas aeruginosa
Management
- See also Carbapenem-resistant organisms
