Structural Organization of theStreptococcus pneumoniaeChromosome and Relatedness of Penicillin-Sensitive and -Resistant Strains in Type 9V
- 1 January 1997
- journal article
- research article
- Published by Mary Ann Liebert Inc in Microbial Drug Resistance
- Vol. 3 (1) , 65-72
- https://doi.org/10.1089/mdr.1997.3.65
Abstract
Fragmentation of Streptococcus pneumoniae genomic DNA with low-frequency-cleavage restriction endonucleases and separation of the fragments by field-inversion gel electrophoresis (FIGE) provides a DNA-finger-print of a strain. This method enables us to construct a physical and genetic map of the R6 laboratory strain what will be presented. The origin of replication containing several Dna boxes was located in the dnaA region. It was of interest to compare the profiles of subclones. Two clones of strain R36A (R6 and Cl3) were cultivated separately for more than 15,000 generations in two laboratories. FIGE profiles differed by only one band. Another R36A descendant, isolated in 1958 by Ravin, strain Rx was of interest since it was deficient in Dpn restriction enzymes and methylases and in the hex B function. Its origin was questionable; its profile is identical to others R6 descendants, demonstrating that Rx is derived from R36A. FIGE analysis was carried out on several penicillin-resistant strains of type 9V because penicillin-resistance in this type increased recently. The profiles of a collection of a number of these resistant isolates were very similar, showing that they result from a clone. The profiles of penicllin sensitive isolates of the same type are very similar to the resistant isolates. This suggests that the 9V type has spread recently from a clone, and the resistance genes have mutated and were selected when penicillin was extensively used.Keywords
This publication has 48 references indexed in Scilit:
- The mmsA locus of Streptococcus pneumoniae encodes a RecG‐like protein involved in DNA repair and in three‐strand recombinationMolecular Microbiology, 1996
- Three Highly Homologous Membrane-bound Lipoproteins Participate in Oligopeptide Transport by the Ami System of the Gram-positive Streptococcus pneumoniaeJournal of Molecular Biology, 1994
- Characterization of the mutX gene of Streptococcus pneumoniae as a homologue of Escherichia coli mutT, and tentative definition of a catalytic domain of the dGTP pyrophosphohydroiasesMolecular Microbiology, 1994
- Structure and function of pneumolysin, the multifunctional, thiol‐activated toxin of Streptococcus pneumoniaeMolecular Microbiology, 1991
- Antigenic Variation of Penicillin-Binding Proteins from Penicillin-Resistant Clinical Strains of Streptococcus pneumoniaeThe Journal of Infectious Diseases, 1991
- Excision-repair capacity in Streptococcus pneumoniae: cloning and expression of a uvr-like geneMutation Research/DNA Repair, 1990
- The ami locus of the Gram‐positive bacterium Streptococcus pneumoniae is similar to binding protein‐dependent transport operons of Gram‐negative bacteriaMolecular Microbiology, 1990
- Nucleotide sequences of the pbpX genes encoding the penicillin‐binding proteins 2x from Streptococcus pneumoniae R6 and a cefotaxime‐resistant mutant, C506Molecular Microbiology, 1989
- Use of insertional inactivation to facilitate studies of biological properties of pneumococcal surface protein A (PspA).The Journal of Experimental Medicine, 1987
- A host-specific variation affecting relative frequency of transformation of two markers in pneumococcusExperimental Cell Research, 1959