Reference : Characterization of an Enterococcus Hirae Penicillin-Binding Protein 3 with Low Penicill...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/81331
Characterization of an Enterococcus Hirae Penicillin-Binding Protein 3 with Low Penicillin Affinity
English
Piras, Graziella [Université de Liège - ULg > Institut de Microbiologie > Service de Microbiologie > >]
El Kharroubi, Aboubaker [Université de Liège - ULg > Institut de Microbiologie > Service de Microbiologie > >]
van Beeumen, Jozef [Rijksuniversiteit-Gent > > Laboratorium voor Mikrobiologie en Microbiële Genetica > >]
Coeme, Etienne [Université de Liège - ULg > Institut de Chimie > Service de Microbiologie > > >]
Coyette, Jacques mailto [Université de Liège - ULg > Institut de Chimie > Service de Microbiologie > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Institut de Chimie > Service de Microbiologie > > >]
1-Dec-1990
Journal of Bacteriology
American Society for Microbiology (ASM)
172
12
6856-6862
Yes (verified by ORBi)
International
0021-9193
1098-5530
Washington
DC
[en] Amino Acid Sequence ; Bacteria/genetics ; Bacteria/metabolism* ; Bacterial Proteins* ; Carrier Proteins* ; Hexosyltransferases/chemistry ; Hexosyltransferases/genetics ; Hexosyltransferases/immunology ; Hexosyltransferases/metabolism* ; Molecular Sequence Data ; Molecular Weight ; Multienzyme Complexes/chemistry ; Multienzyme Complexes/genetics ; Multienzyme Complexes/immunology ; Multienzyme Complexes/metabolism* ; Muramoylpentapeptide Carboxypeptidase* ; Penicillin G/metabolism* ; Penicillin Resistance* ; Penicillin-Binding Proteins ; Peptide Mapping ; Peptidyl Transferases/chemistry ; Peptidyl Transferases/genetics ; Peptidyl Transferases/immunology ; Peptidyl Transferases/metabolism* ; Polymerase Chain Reaction ; Serine Endopeptidases ; Trypsin
[en] Enterococcus hirae S185, a clinical isolate from swine intestine, exhibits a relatively high resistance to penicillin and contains two 77-kDa penicillin-binding proteins 3 of high (PBP 3s) and low (PBP 3r) affinity to penicillin, respectively. A laboratory mutant S185r has been obtained which overproduces PBP 3r and has a highly increased resistance to penicillin. Peptide fragments specifically produced by trypsin and SV8 protease digestions of PBP 3r were isolated, and the amino acid sequences of their amino terminal regions were determined. On the basis of these sequences, oligonucleotides were synthesized and used as primers to generate, by polymerization chain reaction, a 233-bp DNA fragment the sequence of which translated into a 73-amino-acid peptide segment of PBP 3r. These structural data led to the conclusion that the E. hirae PBP 3r and the methicillin-resistant staphylococcal PBP 2' are members of the same class of high-Mr PBPs. As shown by immunological tests, PBP 3r is not related to PBP 3s but, in contrast, is related to the 71-kDa PBP 5 of low penicillin affinity which is responsible for penicillin resistance in E. hirae ATCC 9790 and R40.
Centre d'Ingénierie des Protéines - CIP
Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS ; Fonds de la Recherche Scientifique Médicale - FRSM
Researchers ; Professionals
http://hdl.handle.net/2268/81331

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