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Titolo:
Different penicillin-binding protein profiles in amoxicillin-resistant Helicobacter pylori
Autore:
Dore, MP; Graham, DY; Sepulveda, AR;
Indirizzi:
Vet Affairs Med Ctr, Dept Med, Houston, TX 77030 USA Vet Affairs Med Ctr Houston TX USA 77030 Dept Med, Houston, TX 77030 USA Vet Affairs Med Ctr, Dept Pathol, Houston, TX 77030 USA Vet Affairs Med Ctr Houston TX USA 77030 pt Pathol, Houston, TX 77030 USA Vet Affairs Med Ctr, Div Mol Virol, Houston, TX 77030 USA Vet Affairs Med Ctr Houston TX USA 77030 Mol Virol, Houston, TX 77030 USA Baylor Coll Med, Houston, TX 77030 USA Baylor Coll Med Houston TX USA 77030 ylor Coll Med, Houston, TX 77030 USA
Titolo Testata:
HELICOBACTER
fascicolo: 3, volume: 4, anno: 1999,
pagine: 154 - 161
SICI:
1083-4389(199909)4:3<154:DPPPIA>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI; STAPHYLOCOCCUS-AUREUS; STREPTOCOCCUS-PNEUMONIAE; NEISSERIA-GONORRHOEAE; BETA-LACTAMASES; CELL-SHAPE; TOLERANCE; STRAINS; ANTIBIOTICS; AMPICILLIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Sepulveda, AR Vet Affairs Med Ctr, Dept Med, 111D 2002 Holcombe Blvd, Houston, TX 77030 USA Vet Affairs Med Ctr 111D 2002 Holcombe Blvd Houston TX USA 77030
Citazione:
M.P. Dore et al., "Different penicillin-binding protein profiles in amoxicillin-resistant Helicobacter pylori", HELICOBACT, 4(3), 1999, pp. 154-161

Abstract

Background. The beta-lactam group of antibiotics kills bacteria by inhibiting the terminal stages of peptidoglycan metabolism. We have recently identified amoxicillin-resistant Helicobacter pylori, none of which expressed beta-lactamase. Penicillin-binding proteins (PBPs) represent a group of target enzymes for the beta-lactam antibiotic family, and alterations in PBPs have been described in other penicillin-resistant bacteria. The amoxicillin-resistant phenotype characteristically was lost after freezing but could be restored by consecutive transfers into gradient plates. Materials and Methods. To determine whether amoxicillin resistance in H. pylori was related to alterations in any of the H. pylori PBPs, five H. pylori strains resistant to amoxicillin and three amoxicillin-sensitive strainswere tested. PBPs were extracted from bacteria grown to logarithmic phase,labeled in vivo with H-3-benzylpenicillin, and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and fluorography. Four main PBPs were separated from all amoxicillin-sensitive H. pylori strains. Results. Only three of the four main PBPs were found in the amoxicillin-resistant H. pylori strains. The differentially detectable PBP (PBP D) had anapparent molecular weight of 30 to 32 kD. Conclusion. These results suggest that PBP D might play a role in the amoxicillin-resistant phenotype of H. pylori strains lacking beta-lactamase activity.

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Documento generato il 21/01/21 alle ore 04:25:32