scholarly journals Synthesis, purification and kinetic properties of fluorescein-labelled penicillins

1994 ◽  
Vol 300 (1) ◽  
pp. 141-145 ◽  
Author(s):  
B Lakaye ◽  
C Damblon ◽  
M Jamin ◽  
M Galleni ◽  
S Lepage ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Enterobacter Aerogenes ◽  
Membrane Preparation ◽  
Kinetic Properties ◽  
Bacterial Membrane ◽  
Penicillin Binding Proteins ◽  
Commercial Mixture ◽  
Penicillanic Acid ◽  
Derivatives Of

The synthesis and properties of six fluorescein-labelled penicillins are reported. The two isomers of fluoresceyl-glycyl-6-amino-penicillanic acid are probably the best compounds to use for detection of all the penicillin-binding proteins (PBPs) present in a bacterial membrane preparation. However, the derivatives of ampicillin were much more efficient against Enterobacter aerogenes PBP3. The two isomers obtained when a commercial mixture of the two isomers of carboxyfluorescein was used most often exhibited similar properties, but the Streptomyces R61 extracellular DD-peptidase was only efficiently acylated by the 5′-carboxyfluorescein derivative of glycyl-6-aminopenicillanic acid.

scholarly journals All Detectable High-Molecular-Mass Penicillin-Binding Proteins Are Modified in a High-Level β-Lactam-Resistant Clinical Isolate of Streptococcus mitis

2001 ◽  
Vol 45 (7) ◽  
pp. 2075-2081 ◽  
Author(s):  
Ana Amoroso ◽  
Diego Demares ◽  
Marta Mollerach ◽  
Gabriel Gutkind ◽  
Jacques Coyette
Keyword(s):  
Molecular Mass ◽  
Clinical Isolate ◽  
Active Site ◽  
Binding Proteins ◽  
High Molecular Mass ◽  
Mosaic Structure ◽  
Kinetic Properties ◽  
Streptococcus Mitis ◽  
Penicillin Binding Proteins ◽  
High Level

ABSTRACT All detectable high-molecular-mass penicillin-binding proteins (HMM PBPs) are altered in a clinical isolate of Streptococcus mitis for which the β-lactam MICs are increased from those previously reported in our region (cefotaxime MIC, 64 μg/ml). These proteins were hardly detected at concentrations that saturate all PBPs in clinical isolates and showed, after densitometric analysis, 50-fold-lower radiotracer binding. Resistance was related to mosaic structure in all HMM PBP-coding genes, where critical region replacement was complemented not only by substitutions already reported for the closely related Streptococcus pneumoniae but also by other specific replacements that are presumably close to the active-site serine. Mosaic structure was also presumed in apbp1a-sensitive strain used for comparison, confirming that these structures do not unambiguously imply, by themselves, detectable critical changes in the kinetic properties of these proteins.

scholarly journals Enterobactin- and salmochelin-β-lactam conjugates induce cell morphologies consistent with inhibition of penicillin-binding proteins in uropathogenic Escherichia coli CFT073

2021 ◽  
Author(s):  
Artur Sargun ◽  
Timothy C. Johnstone ◽  
Hui Zhi ◽  
Manuela Raffatellu ◽  
Elizabeth M. Nolan
Keyword(s):  
Escherichia Coli ◽  
Binding Proteins ◽  
Uropathogenic Escherichia Coli ◽  
Penicillin Binding Proteins ◽  
E Coli

Siderophore-β-lactam conjugates based on enterobactin and diglucosylated enterobactin enter the periplasm of uropathogenic E. coli CFT073 via the FepA and IroN transporters, and target penicillin-binding proteins.

scholarly journals Function and Localization Dynamics of Bifunctional Penicillin-Binding Proteins in Caulobacter crescentus

2014 ◽  
Vol 196 (8) ◽  
pp. 1627-1639 ◽  
Author(s):  
W. Strobel ◽  
A. Moll ◽  
D. Kiekebusch ◽  
K. E. Klein ◽  
M. Thanbichler
Keyword(s):  
Binding Proteins ◽  
Caulobacter Crescentus ◽  
Penicillin Binding Proteins

scholarly journals Interaction of β-lactam antibiotics with penicillin-binding proteins fromPseudomonas aeruginosa

1982 ◽  
Vol 14 (4) ◽  
pp. 295-298 ◽  
Author(s):  
Alfredo Rodriguez-Tebár ◽  
Fernando Rojo ◽  
Juan C. Montilla ◽  
David Vázquez
Keyword(s):  
Binding Proteins ◽  
Penicillin Binding Proteins

scholarly journals Increasing Ceftriaxone Resistance and Multiple Alterations of Penicillin-Binding Proteins among Penicillin-Resistant Streptococcus pneumoniae Isolates in Taiwan

2007 ◽  
Vol 51 (9) ◽  
pp. 3404-3406 ◽  
Author(s):  
Cheng-Hsun Chiu ◽  
Lin-Hui Su ◽  
Yhu-Chering Huang ◽  
Jui-Chia Lai ◽  
Hsiu-Ling Chen ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Amino Acid ◽  
Binding Proteins ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Penicillin Binding Proteins

ABSTRACT The rate of nonsusceptibility of penicillin-resistant Streptococcus pneumoniae strains to ceftriaxone increased significantly in Taiwan in 2005. Approximately 90% of the ceftriaxone-nonsusceptible isolates were found to be of four major serotypes (serotypes 6B, 14, 19F, and 23F). Seven amino acid alterations in the penicillin-binding protein 2B transpeptidase-encoding region specifically contributed to the resistance.

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