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Resistance to antibiotics mediated by target alterations.
- Source :
-
Science (New York, N.Y.) [Science] 1994 Apr 15; Vol. 264 (5157), pp. 388-93. - Publication Year :
- 1994
-
Abstract
- The development of resistance to antibiotics by reductions in the affinities of their enzymatic targets occurs most rapidly for antibiotics that inactivate a single target and that are not analogs of substrate. In these cases of resistance (for example, resistance to rifampicin), numerous single amino acid substitutions may provide large decreases in the affinity of the target for the antibiotic, leading to clinically significant levels of resistance. Resistance due to target alterations should occur much more slowly for those antibiotics (penicillin, for example) that inactivate multiple targets irreversibly by acting as close analogs of substrate. Resistance to penicillin because of target changes has emerged, by unexpected mechanisms, only in a limited number of species. However, inactivating enzymes commonly provide resistance to antibiotics that, like penicillin, are derived from natural products, although such enzymes have not been found for synthetic antibiotics. Thus, the ideal antibiotic would be produced by rational design, rather than by the modification of a natural product.
- Subjects :
- 4-Quinolones
Amino Acid Sequence
Anti-Infective Agents pharmacology
Bacteria genetics
Bacteria metabolism
Carrier Proteins genetics
Lactams
Molecular Sequence Data
Muramoylpentapeptide Carboxypeptidase genetics
Neisseria drug effects
Neisseria genetics
Neisseria metabolism
Penicillin Resistance
Penicillin-Binding Proteins
Recombination, Genetic
Rifampin pharmacology
Staphylococcus aureus drug effects
Staphylococcus aureus genetics
Staphylococcus aureus metabolism
Streptococcus pneumoniae drug effects
Streptococcus pneumoniae genetics
Streptococcus pneumoniae metabolism
Anti-Bacterial Agents pharmacology
Bacteria drug effects
Bacterial Proteins
Carrier Proteins metabolism
Drug Resistance, Microbial
Hexosyltransferases
Muramoylpentapeptide Carboxypeptidase metabolism
Peptidyl Transferases
Subjects
Details
- Language :
- English
- ISSN :
- 0036-8075
- Volume :
- 264
- Issue :
- 5157
- Database :
- MEDLINE
- Journal :
- Science (New York, N.Y.)
- Publication Type :
- Academic Journal
- Accession number :
- 8153626
- Full Text :
- https://doi.org/10.1126/science.8153626