Penicillin-binding proteins and ampicillin resistance in Haemophilus influenzae.
J Antimicrob Chemother
; 25(4): 525-34, 1990 Apr.
Article
en En
| MEDLINE
| ID: mdl-2351623
ABSTRACT
Ampicillin-resistant, non-beta-lactamase-producing isolates of Haemophilus influenzae contain a variety of penicillin-binding protein (PBP) patterns that differ from the single pattern of eight PBPs characteristic of susceptible strains. During genetic transformation of resistance, only some of the anomalies in PBP pattern were transformed, specifically those relating to the penicillin-binding capacities of PBPs 4 (Mr of 62,000) and 5 (Mr of 59,000) and, in some transformations, PBP 3 (Mr of 71,000). Comparison of the binding of penicillin by PBPs 4 and 5 of three resistant transformants (derived with DNA from different donors) revealed a decrease in the rate of PBP acylation and no appreciable change in the rate of deacylation as compared to the susceptible recipient. Thus, rapid turnover of these PBPs does not play a role. Retransformation studies confirm that altered PBPs 3, 4, and 5 are associated with resistance and suggest that these PBPs are major targets for the beta-lactam antibiotics in H. influenzae.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Penicilinas
/
Proteínas Bacterianas
/
Resistencia a la Ampicilina
/
Muramoilpentapéptido Carboxipeptidasa
/
Proteínas Portadoras
/
Peptidil Transferasas
/
Haemophilus influenzae
/
Hexosiltransferasas
Idioma:
En
Revista:
J Antimicrob Chemother
Año:
1990
Tipo del documento:
Article