Zobrazeno 1 - 10
of 318
pro vyhledávání: '"R, Hakenbeck"'
Publikováno v:
Iranian Journal of Microbiology, Vol 3, Iss 2 (2011)
Background and objectives: Streptococcus pneumoniae, a major human pathogen, is closely related to the commensal species S. mitis and S. oralis. S. pneumoniae surface proteins are implicated in virulence and host interaction of this species, but many
Externí odkaz:
https://doaj.org/article/e4f58ac093214ce29bce6cd75a7b0be0
Autor:
J. Coyette, R. Hakenbeck
Publikováno v:
Cellular and Molecular Life Sciences CMLS. 54:332-340
Low-affinity penicillin-binding proteins (PBPs), which participate in the beta-lactam resistance of several pathogenic bacteria, have different origins. Natural transformation and recombination events with DNA acquired from neighbouring intrinsically
Publikováno v:
Iranian Journal of Microbiology
Background and objectives Streptococcus pneumoniae, a major human pathogen, is closely related to the commensal species S. mitis and S. oralis. S. pneumoniae surface proteins are implicated in virulence and host interaction of this species, but many
Autor:
R, Hakenbeck
Publikováno v:
Methods in molecular medicine. 48
Penicillin-resistance in Streptococcus pneumoniae is mediated by altered penicillin-target enzymes, the penicillin-binding proteins or PBPs. PBPs interact withβ-lactam antibiotics by forming an active penicilloyl-PBP complex via an active site serin
Publikováno v:
Biochemical Journal. 292:735-741
The high-molecular-mass penicillin-binding protein (PBP) 2x, one of the primary targets of beta-lactam antibiotics in Streptococcus pneumoniae, has been produced as a soluble form and purified in large amounts. It has been shown to catalyse hydrolysi
Publikováno v:
Antimicrobial Agents and Chemotherapy. 36:783-787
In 1989 and 1990, a large number of ampicillin-resistant strains of Enterococcus faecium were isolated from infected patients treated at intensive care units in Berlin, Germany. Twenty-five clinical isolates, including five different biotypes as clas
Publikováno v:
The Journal of biological chemistry. 274(27)
Penicillin-binding protein 2x (PBP2x) isolated from clinical beta-lactam-resistant strains of Streptococcus pneumoniae (R-PBP2x) have a reduced affinity for beta-lactam antibiotics. Their transpeptidase domain carries numerous substitutions compared
Autor:
R, Hakenbeck
Publikováno v:
Chemotherapy. 45(2)
Autor:
R, Hakenbeck
Publikováno v:
Electrophoresis. 19(4)
Penicillin resistance in clinical isolates of Streptococcus pneumoniae is mediated by mosaic genes encoding altered penicillin binding proteins. Mosaic sequence blocks are the result of a genetic exchange between related streptococcal species. It is
Autor:
R, Hakenbeck, A, König, I, Kern, M, van der Linden, W, Keck, D, Billot-Klein, R, Legrand, B, Schoot, L, Gutmann
Publikováno v:
Journal of bacteriology. 180(7)
Penicillin-resistant isolates of Streptococcus pneumoniae generally contain mosaic genes encoding the low-affinity penicillin-binding proteins (PBPs) PBP2x, PBP2b, and PBP1a. We now present evidence that PBP2a and PBP1b also appear to be low-affinity