BIOMAT Database Logo BIOMAT Database Logo

Acquisition of five high-Mr penicillin-binding protein variants during transfer of high-level beta-lactam resistance from Streptococcus mitis to Streptococcus pneumoniae. 1998

R Hakenbeck, and A König, and I Kern, and M van der Linden, and W Keck, and D Billot-Klein, and R Legrand, and B Schoot, and L Gutmann
Max-Planck Institut für Molekulare Genetik, Berlin, Germany. hakenb@rhrk.uni-kl.de

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 variants and are encoded by distinct alleles in beta-lactam-resistant transformants of S. pneumoniae obtained with chromosomal donor DNA from a Streptococcus mitis isolate. Different lineages of beta-lactam-resistant pneumococcal transformants were analyzed, and transformants with low-affinity variants of all high-molecular-mass PBPs, PBP2x, -2a, -2b, -1a, and -1b, were isolated. The MICs of benzyl-penicillin, oxacillin, and cefotaxime for these transformants were up to 40, 100, and 50 microg/ml, respectively, close to the MICs for the S. mitis donor strain. Recruitment of low-affinity PBPs was accompanied by a decrease in cross-linked muropeptides as revealed by high-performance liquid chromatography of muramidase-digested cell walls, but no qualitative changes in muropeptide chemistry were detected. The growth rates of all transformants were identical to that of the parental S. pneumoniae strain. The results stress the potential for the acquisition by S. pneumoniae of high-level beta-lactam resistance by interspecies gene transfer.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D010403 Penicillin Resistance Nonsusceptibility of an organism to the action of penicillins. Penicillin Resistances,Resistance, Penicillin,Resistances, Penicillin
D010453 Peptide Synthases Ligases that catalyze the joining of adjacent AMINO ACIDS by the formation of carbon-nitrogen bonds between their carboxylic acid groups and amine groups. Peptide Synthetases,Acid-Amino-Acid Ligases,Acid Amino Acid Ligases,Ligases, Acid-Amino-Acid,Synthases, Peptide,Synthetases, Peptide
D010458 Peptidyl Transferases Acyltransferases that use AMINO ACYL TRNA as the amino acid donor in formation of a peptide bond. There are ribosomal and non-ribosomal peptidyltransferases. Peptidyl Transferase,Peptidyl Translocase,Peptidyl Translocases,Peptidyltransferase,Transpeptidase,Transpeptidases,Peptidyltransferases,Transferase, Peptidyl,Transferases, Peptidyl,Translocase, Peptidyl,Translocases, Peptidyl
D002267 Muramoylpentapeptide Carboxypeptidase Enzyme which catalyzes the peptide cross-linking of nascent CELL WALL; PEPTIDOGLYCAN. Carboxypeptidase Transpeptidase,Carboxypeptidase, Muramoylpentapeptide,Transpeptidase, Carboxypeptidase
D002352 Carrier Proteins Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D002439 Cefotaxime Semisynthetic broad-spectrum cephalosporin. Benaxima,Biosint,Cefotaxim,Cefotaxime Sodium,Cefradil,Cephotaxim,Claforan,Fotexina,HR-756,Kendrick,Klaforan,Primafen,Ru-24756,Taporin,HR 756,HR756,Ru 24756,Ru24756,Sodium, Cefotaxime
D004352 Drug Resistance, Microbial The ability of microorganisms, especially bacteria, to resist or to become tolerant to chemotherapeutic agents, antimicrobial agents, or antibiotics. This resistance may be acquired through gene mutation or foreign DNA in transmissible plasmids (R FACTORS). Antibiotic Resistance,Antibiotic Resistance, Microbial,Antimicrobial Resistance, Drug,Antimicrobial Drug Resistance,Antimicrobial Drug Resistances,Antimicrobial Resistances, Drug,Drug Antimicrobial Resistance,Drug Antimicrobial Resistances,Drug Resistances, Microbial,Resistance, Antibiotic,Resistance, Drug Antimicrobial,Resistances, Drug Antimicrobial
D006602 Hexosyltransferases Enzymes that catalyze the transfer of hexose groups. EC 2.4.1.-.

Related Publications

R Hakenbeck, and A König, and I Kern, and M van der Linden, and W Keck, and D Billot-Klein, and R Legrand, and B Schoot, and L Gutmann
beta-lactam resistance in Streptococcus pneumoniae: penicillin-binding proteins and non-penicillin-binding proteins.
August 1999, Molecular microbiology,
R Hakenbeck, and A König, and I Kern, and M van der Linden, and W Keck, and D Billot-Klein, and R Legrand, and B Schoot, and L Gutmann
Penicillin binding protein 2x as a major contributor to intrinsic beta-lactam resistance of Streptococcus pneumoniae.
September 1993, FEBS letters,
R Hakenbeck, and A König, and I Kern, and M van der Linden, and W Keck, and D Billot-Klein, and R Legrand, and B Schoot, and L Gutmann
Biochemical characterization of Streptococcus pneumoniae penicillin-binding protein 2b and its implication in beta-lactam resistance.
May 2004, Antimicrobial agents and chemotherapy,
R Hakenbeck, and A König, and I Kern, and M van der Linden, and W Keck, and D Billot-Klein, and R Legrand, and B Schoot, and L Gutmann
Kinetics of beta-lactam interactions with penicillin-susceptible and -resistant penicillin-binding protein 2x proteins from Streptococcus pneumoniae. Involvement of acylation and deacylation in beta-lactam resistance.
August 2001, The Journal of biological chemistry,
R Hakenbeck, and A König, and I Kern, and M van der Linden, and W Keck, and D Billot-Klein, and R Legrand, and B Schoot, and L Gutmann
All detectable high-molecular-mass penicillin-binding proteins are modified in a high-level beta-lactam-resistant clinical isolate of Streptococcus mitis.
July 2001, Antimicrobial agents and chemotherapy,
R Hakenbeck, and A König, and I Kern, and M van der Linden, and W Keck, and D Billot-Klein, and R Legrand, and B Schoot, and L Gutmann
Relatedness among penicillin-binding protein 2b genes of Streptococcus mitis, Streptococcus oralis, and Streptococcus pneumoniae.
January 1995, Microbial drug resistance (Larchmont, N.Y.),
R Hakenbeck, and A König, and I Kern, and M van der Linden, and W Keck, and D Billot-Klein, and R Legrand, and B Schoot, and L Gutmann
New Insights into Beta-Lactam Resistance of Streptococcus pneumoniae: Serine Protease HtrA Degrades Altered Penicillin-Binding Protein 2x.
August 2021, Microorganisms,
R Hakenbeck, and A König, and I Kern, and M van der Linden, and W Keck, and D Billot-Klein, and R Legrand, and B Schoot, and L Gutmann
Endocarditis due to Streptococcus mitis with high-level resistance to penicillin and ceftriaxone.
May 2001, JAMA,
R Hakenbeck, and A König, and I Kern, and M van der Linden, and W Keck, and D Billot-Klein, and R Legrand, and B Schoot, and L Gutmann
Endocarditis due to Streptococcus mitis with high-level resistance to penicillin and cefotaxime.
October 1999, The New England journal of medicine,
R Hakenbeck, and A König, and I Kern, and M van der Linden, and W Keck, and D Billot-Klein, and R Legrand, and B Schoot, and L Gutmann
Identical penicillin-binding domains in penicillin-binding proteins of Streptococcus pneumoniae clinical isolates with different levels of beta-lactam resistance.
July 2005, Antimicrobial agents and chemotherapy,
Copied contents to your clipboard!