scholarly journals Mutation in 23S rRNA Responsible for Resistance to 16-Membered Macrolides and Streptogramins in Streptococcus pneumoniae

2001 ◽  
Vol 45 (1) ◽  
pp. 319-323 ◽  
Author(s):  
Florence Depardieu ◽  
Patrice Courvalin
Keyword(s):  
Escherichia Coli ◽  
Streptococcus Pneumoniae ◽  
Clinical Isolate ◽  
23S Rrna ◽  
Resistance Phenotype ◽  
Domain V

ABSTRACT Streptococcus pneumoniae clinical isolate BM4455 was resistant to 16-membered macrolides and to streptogramins. This unusual resistance phenotype was due to an A2062C (Escherichia coli numbering) mutation in domain V of the four copies of 23S rRNA.

scholarly journals Ribosomal Mutations in Streptococcus pneumoniae Clinical Isolates

2002 ◽  
Vol 46 (3) ◽  
pp. 654-658 ◽  
Author(s):  
Marja Pihlajamäki ◽  
Janne Kataja ◽  
Helena Seppälä ◽  
John Elliot ◽  
Maija Leinonen ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Ribosomal Protein ◽  
Resistance Genes ◽  
Macrolide Resistance ◽  
Clinical Isolates ◽  
23S Rrna ◽  
Resistance Phenotype ◽  
Low Level ◽  
Domain V

ABSTRACT Eleven clinical isolates of Streptococcus pneumoniae, isolated in Finland during 1996 to 2000, had an unusual macrolide resistance phenotype. They were resistant to macrolides and streptogramin B but susceptible, intermediate, or low-level resistant to lincosamides. No acquired macrolide resistance genes were detected from the strains. The isolates were found to have mutations in domain V of the 23S rRNA or ribosomal protein L4. Seven isolates had an A2059C mutation in two to four out of the four alleles encoding the 23S rRNA, two isolates had an A2059G mutation in two alleles, one isolate had a C2611G mutation in all four alleles, and one isolate had a 69GTG71-to-69TPS71 substitution in ribosomal protein L4.

scholarly journals Protein Folding by Domain V of Escherichia coli 23S rRNA: Specificity of RNA-Protein Interactions

2008 ◽  
Vol 190 (9) ◽  
pp. 3344-3352 ◽  
Author(s):  
Dibyendu Samanta ◽  
Debashis Mukhopadhyay ◽  
Saheli Chowdhury ◽  
Jaydip Ghosh ◽  
Saumen Pal ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Folding ◽  
Carbonic Anhydrase ◽  
Protein Interactions ◽  
23S Rrna ◽  
Unfolded Proteins ◽  
Bovine Carbonic Anhydrase ◽  
Egg White Lysozyme ◽  
General Protein ◽  
Domain V

ABSTRACT The peptidyl transferase center, present in domain V of 23S rRNA of eubacteria and large rRNA of plants and animals, can act as a general protein folding modulator. Here we show that a few specific nucleotides in Escherichia coli domain V RNA bind to unfolded proteins and, as shown previously, bring the trapped proteins to a folding-competent state before releasing them. These nucleotides are the same for the proteins studied so far: bovine carbonic anhydrase, lactate dehydrogenase, malate dehydrogenase, and chicken egg white lysozyme. The amino acids that interact with these nucleotides are also found to be specific in the two cases tested: bovine carbonic anhydrase and lysozyme. They are either neutral or positively charged and are present in random coils on the surface of the crystal structure of both the proteins. In fact, two of these amino acid-nucleotide pairs are identical in the two cases. How these features might help the process of protein folding is discussed.

scholarly journals Resistance of Streptococcus pneumoniaeto Deformylase Inhibitors Is Due to Mutations indefB

2001 ◽  
Vol 45 (9) ◽  
pp. 2432-2435 ◽  
Author(s):  
Peter Margolis ◽  
Corinne Hackbarth ◽  
Sara Lopez ◽  
Mita Maniar ◽  
Wen Wang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Staphylococcus Aureus ◽  
Streptococcus Pneumoniae ◽  
Peptide Deformylase ◽  
Wild Type ◽  
Resistance Phenotype ◽  
Resistant Mutants

ABSTRACT Resistance to peptide deformylase inhibitors in Escherichia coli or Staphylococcus aureus is due to inactivation of transformylase activity. Knockout experiments in Streptococcus pneumoniae R6x indicate that the transformylase (fmt) and deformylase (defB) genes are essential and that adef paralog (defA) is not. Actinonin-resistant mutants of S. pneumoniae ATCC 49619 harbor mutations indefB but not in fmt. Reintroduction of the mutated defB gene into wild-type S. pneumoniaeR6x recreates the resistance phenotype. The altered enzyme displays decreased sensitivity to actinonin.

scholarly journals Heterogeneous Macrolide Resistance and Gene Conversion in the Pneumococcus

2006 ◽  
Vol 50 (1) ◽  
pp. 359-361 ◽  
Author(s):  
Nicole Wolter ◽  
Anthony M. Smith ◽  
David J. Farrell ◽  
Keith P. Klugman
Keyword(s):  
Streptococcus Pneumoniae ◽  
Gene Conversion ◽  
Clinical Isolate ◽  
Resistant Strain ◽  
Macrolide Resistance ◽  
Fitness Cost ◽  
Rrna Genes ◽  
23S Rrna ◽  
Resistant Phenotype ◽  
23S Rrna Genes

ABSTRACT A macrolide-resistant clinical isolate of Streptococcus pneumoniae with 23S rRNA mutations showed a heterogeneous phenotype and genotype. The mutant 23S rRNA genes from this isolate transformed susceptible strain R6 to resistance. Culture of resistant strain R6 in the absence of antibiotic pressure showed gene conversion to occur between the four 23S rRNA alleles, resulting in reversion to susceptibility with the resistant phenotype showing a fitness cost. These data explain the disappearance on subculture of heterogeneous macrolide resistance in the pneumococcus.

scholarly journals Methylation of 23S rRNA Nucleotide G748 by RlmAIIMethyltransferase Renders Streptococcus pneumoniae Telithromycin Susceptible

2013 ◽  
Vol 57 (8) ◽  
pp. 3789-3796 ◽  
Author(s):  
Akiko Takaya ◽  
Yoshiharu Sato ◽  
Tatsuma Shoji ◽  
Tomoko Yamamoto
Keyword(s):  
Streptococcus Pneumoniae ◽  
Stop Codon ◽  
Regulatory Region ◽  
Dimethyl Sulfate ◽  
23S Rrna ◽  
Gene Encoding ◽  
Content Type ◽  
Resistant Mutants ◽  
High Level ◽  
Domain V

ABSTRACTSeveral posttranscriptional modifications of bacterial rRNAs are important in determining antibiotic resistance or sensitivity. In all Gram-positive bacteria, dimethylation of nucleotide A2058, located in domain V of 23S rRNA, by the dimethyltransferase Erm(B) results in low susceptibility and resistance to telithromycin (TEL). However, this is insufficient to produce high-level resistance to TEL inStreptococcus pneumoniae. Inactivation of the methyltransferase RlmAII, which methylates the N-1 position of nucleotide G748, located in hairpin 35 of domain II of 23S rRNA, results in increased resistance to TEL inerm(B)-carryingS. pneumoniae. Sixteen TEL-resistant mutants (MICs, 16 to 32 μg/ml) were obtained from a clinically isolatedS. pneumoniaestrain showing low TEL susceptibility (MIC, 2 μg/ml), with mutation resulting in constitutive dimethylation of A2058 because of nucleotide differences in the regulatory region oferm(B) mRNA. Primer extension analysis showed that the degree of methylation at G748 in all TEL-resistant mutants was significantly reduced by a mutation in the gene encoding RlmAIIto create a stop codon or change an amino acid residue. Furthermore, RNA footprinting with dimethyl sulfate and a molecular modeling study suggested that methylation of G748 may contribute to the stable interaction of TEL with domain II of 23S rRNA, even after dimethylation of A2058 by Erm(B). This novel finding shows that methylation of G748 by RlmAIIrendersS. pneumoniaeTEL susceptible.

scholarly journals Ribosomal Mutations Conferring Resistance to Macrolides in Streptococcus pneumoniae Clinical Strains Isolated in Germany

2003 ◽  
Vol 47 (7) ◽  
pp. 2319-2322 ◽  
Author(s):  
Ralf René Reinert ◽  
Angela Wild ◽  
Peter Appelbaum ◽  
Rudolf Lütticken ◽  
Murat Yücel Cil ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Amino Acid ◽  
Ribosomal Protein ◽  
Macrolide Resistance ◽  
23S Rrna ◽  
Resistance Phenotype ◽  
Clinical Strains ◽  
Acid Alteration ◽  
Amino Acid Alteration

ABSTRACT Among a collection of 4,281 pneumococcal isolates, 7 strains isolated in Germany had an unusual macrolide resistance phenotype. The isolates were found to have multiple mutations in the 23S rRNA and alterations in the L4 ribosomal protein. One strain had an amino acid alteration in the L22 ribosomal protein.

scholarly journals Genetic and Biochemical Characterization of a Chromosome-Encoded Carbapenem-Hydrolyzing Ambler Class D β-Lactamase from Shewanella algae

2004 ◽  
Vol 48 (5) ◽  
pp. 1670-1675 ◽  
Author(s):  
Claire Héritier ◽  
Laurent Poirel ◽  
Patrice Nordmann
Keyword(s):  
Escherichia Coli ◽  
Clinical Isolate ◽  
Biochemical Characterization ◽  
Resistance Phenotype ◽  
Narrow Spectrum ◽  
Class D ◽  
Shewanella Algae ◽  
Lactamase Gene

ABSTRACT A chromosome-encoded β-lactamase gene from Shewanella algae clinical isolate KB-1 was cloned and expressed in Escherichia coli. It encoded the Ambler class D enzyme OXA-55, sharing less than 55% identity with any other oxacillinases. Although conferring a narrow-spectrum β-lactam resistance phenotype, OXA-55 had carbapenem-hydrolyzing activity that mirrored the reduced susceptibility to imipenem observed in S. algae KB-1. Very similar oxacillinases were found in other S. algae isolates.

scholarly journals Mutations in 23S rRNA are associated with clarithromycin resistance in Helicobacter pylori.

1996 ◽  
Vol 40 (2) ◽  
pp. 477-480 ◽  
Author(s):  
J Versalovic ◽  
D Shortridge ◽  
K Kibler ◽  
M V Griffy ◽  
J Beyer ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Helicobacter Pylori ◽  
Peptic Ulcer ◽  
23S Rrna ◽  
Treatment Regimens ◽  
Clarithromycin Resistance ◽  
Transition Mutation ◽  
H Pylori ◽  
Domain V ◽  
Ulcer Treatment

Twelve clarithromycin-resistant Helicobacter pylori isolates (100% of resistant isolates examined) from seven different patients each contained an A-->G transition mutation within a conserved loop of 23S rRNA. A-->G transition mutations at positions cognate with Escherichia coli 23S rRNA positions 2058 and 2059 were identified. Clarithromycin-susceptible H. pylori isolates from 14 different patients displayed no polymorphisms in a conserved loop within domain V of 23S rRNA. The study is the first to report mutations in H. pylori associated with resistance to an antimicrobial agent used in established peptic ulcer treatment regimens.

scholarly journals Macrolide-Resistant and Macrolide-Sensitive Mycoplasma pneumoniae Pneumonia in Children Treated Using Early Corticosteroids

2021 ◽  
Vol 10 (6) ◽  
pp. 1309
Author(s):  
Hye Young Han ◽  
Ki Cheol Park ◽  
Eun-Ae Yang ◽  
Kyung-Yil Lee
Keyword(s):  
Mycoplasma Pneumoniae ◽  
Serological Test ◽  
Corticosteroid Treatment ◽  
23S Rrna ◽  
Laboratory Parameters ◽  
The Mean ◽  
Domain V ◽  
Positive Results ◽  
Mycoplasma Pneumoniae Pneumonia

We have found that early corticosteroid therapy was effective for reducing morbidity during five Korea-wide epidemics. We evaluated the clinical and laboratory parameters of 56 children who received early corticosteroid treatment for pneumonia that was caused by macrolide-resistant Mycoplasma pneumoniae (M. pneumoniae) or macrolide-sensitive M. pneumoniae between July 2019 and February 2020. All subjects had dual positive results from a PCR assay and serological test, and received corticosteroids within 24–36 h after admission. Point mutation of residues 2063, 2064, and 2067 was identified in domain V of 23S rRNA. The mean age was 6.8 years and the male:female ratio was 1.2:1 (31:25 patients). Most of the subjects had macrolide-resistant M. pneumoniae (73%), and all mutated strains had the A2063G transition. No significant differences in clinical and laboratory parameters were observed between macrolide-resistant and macrolide-sensitive M. pneumoniae groups that were treated with early dose-adjusted corticosteroids. Higher-dose steroid treatment may be needed for patients who have fever that persists for >48 h or increased biomarkers such as lactate dehydrogenase concentration at follow-up despite a usual dose of steroid therapy.

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