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Updated: Oct 16, 2026

Isolation and Identification of Waterborne Antibiotic-Resistant Bacteria and Molecular Characterization of their Antibiotic Resistance Genes
Published on: March 3, 2023
[Drug-resistant bacteria of current topics and their resistance mechanisms--PRSP and BLNAR]
Abstract:
The prevalence of resistant isolates for beta-lactam antibiotics have been rapidly increasing in Streptococcus pneumoniae and Haemophilus influenzae. These strains having resistant elements are called penicillin-resistant S. pneumoniae(PRSP) and beta-lactamase-negative ampicillin-resistant H. influenzae(BLNAR). The mechanism of resistance was identified as the reduction of penicillin-binding proteins(PBPs) affinities as the target of beta-lactams. In PRSP, pbp1a, pbp2x, and pbp2b encoding PBP1A, -2X, and -2B enzymes, respectively, were altered. In contrast, mutations in the ftsI gene encoding PBP3A were only clarified in BLNAR. Characteristics of the resistance caused by PBPs alterations are a low-level resistance that decrease bactericidal action.
Insights
Antibiotic resistance is rising in Streptococcus pneumoniae and Haemophilus influenzae due to altered penicillin-binding proteins (PBPs). This impacts treatment effectiveness, particularly for beta-lactam antibiotics.
Area of Science:
- Microbiology
- Molecular Biology
- Infectious Diseases
Background:
- Increasing prevalence of beta-lactam antibiotic resistance in Streptococcus pneumoniae and Haemophilus influenzae.
- Identification of resistant strains as penicillin-resistant S. pneumoniae (PRSP) and beta-lactamase-negative ampicillin-resistant H. influenzae (BLNAR).
Purpose of the Study:
- To investigate the molecular mechanisms of beta-lactam resistance in PRSP and BLNAR.
- To identify specific alterations in penicillin-binding proteins (PBPs) responsible for resistance.
Main Methods:
- Analysis of genetic mutations in genes encoding PBPs in resistant bacterial isolates.
- Comparison of PBP alterations between PRSP and BLNAR strains.
Main Results:
- Penicillin-resistant S. pneumoniae (PRSP) showed alterations in pbp1a, pbp2x, and pbp2b genes, affecting PBP1A, -2X, and -2B.
- Beta-lactamase-negative ampicillin-resistant H. influenzae (BLNAR) exhibited mutations exclusively in the ftsI gene, encoding PBP3A.
- PBP alterations result in low-level antibiotic resistance, diminishing the bactericidal effect of beta-lactams.
Conclusions:
- Distinct PBP alteration mechanisms drive beta-lactam resistance in S. pneumoniae and H. influenzae.
- Understanding these mechanisms is crucial for developing effective antimicrobial strategies against resistant bacterial infections.
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