Article (Scientific journals)
Characterization of an Enterococcus Hirae Penicillin-Binding Protein 3 with Low Penicillin Affinity
Piras, Graziella; El Kharroubi, Aboubaker; van Beeumen, Jozef et al.
1990In Journal of Bacteriology, 172 (12), p. 6856-6862
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Keywords :
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
Abstract :
[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.
Research center :
CIP - Centre d'Ingénierie des Protéines - ULiège
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Piras, Graziella;  Université de Liège - ULiège > Institut de Microbiologie > Service de Microbiologie
El Kharroubi, Aboubaker;  Université de Liège - ULiège > Institut de Microbiologie > Service de Microbiologie
van Beeumen, Jozef;  Rijksuniversiteit-Gent > Laboratorium voor Mikrobiologie en Microbiële Genetica
Coeme, Etienne;  Université de Liège - ULiège > Institut de Chimie > Service de Microbiologie
Coyette, Jacques ;  Université de Liège - ULiège > Institut de Chimie > Service de Microbiologie
Ghuysen, Jean-Marie ;  Université de Liège - ULiège > Institut de Chimie > Service de Microbiologie
Language :
English
Title :
Characterization of an Enterococcus Hirae Penicillin-Binding Protein 3 with Low Penicillin Affinity
Publication date :
01 December 1990
Journal title :
Journal of Bacteriology
ISSN :
0021-9193
eISSN :
1098-5530
Publisher :
American Society for Microbiology (ASM), Washington, United States - District of Columbia
Volume :
172
Issue :
12
Pages :
6856-6862
Peer reviewed :
Peer Reviewed verified by ORBi
Funders :
F.R.S.-FNRS - Fonds de la Recherche Scientifique [BE]
FRSM - Fonds de la Recherche Scientifique Médicale [BE]
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