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Variability of penicillin-binding proteins from penicillin-sensitive Streptococcus pneumoniae
R Hakenbeck1, T Briese, L Chalkley
1Max-Planck Institut für Molekulare Genetik, Berlin, Germany.
The Journal of Infectious Diseases
|August 1, 1991
Summary
Penicillin-susceptible Streptococcus pneumoniae strains show unexpected variation in penicillin-binding proteins (PBPs). Antigenic and electrophoretic differences in PBPs 1a and 2b were observed, even within the same sero-group.
Area of Science:
- Microbiology
- Immunology
- Molecular Biology
Background:
- Penicillin-binding proteins (PBPs) are crucial targets for beta-lactam antibiotics.
- PBPs in penicillin-susceptible Streptococcus pneumoniae are generally considered similar.
- Variations in PBPs can contribute to antibiotic resistance mechanisms.
Purpose of the Study:
- To analyze the antigenic variation of PBPs 1a and 2b in penicillin-susceptible Streptococcus pneumoniae.
- To compare PBP profiles between susceptible and resistant isolates.
Main Methods:
- Analysis of antigenic variation using specific antisera and monoclonal antibodies.
- Electrophoretic comparison of all six PBPs via SDS-PAGE and fluorography.
Main Results:
- Three strains exhibited distinct antigenic variants of PBP 1a.
- Fifty strains displayed one of three antigenic variants for PBP 2b.
- Seven antibody reactivity patterns were identified, mostly differing from resistant strains.
- Electrophoresis revealed unexpected PBP profile variations, even within sero-groups.
Conclusions:
- Penicillin-susceptible Streptococcus pneumoniae strains harbor significant antigenic and electrophoretic diversity in PBPs.
- This PBP variability may have implications for understanding pneumococcal evolution and antibiotic susceptibility.
- Further research is needed to elucidate the functional significance of these PBP variations.