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Characterization of high-level aminoglycoside resistance in a strain of Streptococcus pneumoniae
Abstract:
The aminoglycoside phosphotransferase (APH)(3')(5'')-III has been characterized from Streptococcus pneumoniae BM4200, which is resistant to high levels of aminoglycosides. The phosphotransferase was apparently chromosomally-encoded and was responsible for the high-level resistance. The enzyme was not notably pH-dependent, was heterogeneous after isoelectric focusing, with pI values of approximately 4.8 and 5.1, and had an apparent molecular weight of 32 500 after SDS-PAGE.
Insights
Streptococcus pneumoniae BM4200 possesses a chromosomally-encoded aminoglycoside phosphotransferase (APH)(3')(5')-III enzyme, conferring high-level aminoglycoside resistance. This enzyme
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- Aminoglycoside resistance is a significant clinical challenge.
- Streptococcus pneumoniae is a major human pathogen.
- Understanding resistance mechanisms is crucial for developing new therapies.
Purpose of the Study:
- To characterize the aminoglycoside phosphotransferase (APH)(3")(5")-III enzyme from Streptococcus pneumoniae BM4200.
- To elucidate the role of this enzyme in high-level aminoglycoside resistance.
Main Methods:
- Enzyme characterization
- Isoelectric focusing (IEF)
- Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE)
Main Results:
- The enzyme, APH(3")(5")-III, was identified as the cause of high-level aminoglycoside resistance.
- The enzyme is chromosomally encoded.
- It exhibited pH stability and heterogeneity with pI values of approximately 4.8 and 5.1.
- Apparent molecular weight was determined to be 32,500 Da via SDS-PAGE.
Conclusions:
- APH(3")(5")-III is responsible for high-level aminoglycoside resistance in S. pneumoniae BM4200.
- The enzyme's characteristics provide insights into its function and potential inhibition strategies.