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A Liposome Membrane Permeability Assay for Investigating the Effects of Phosphatidylinositol Phosphate Groups on Membranotropic Action of Venom PLA2

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Multiple extracellular phospholipase activities from Prevotella intermedia.

Jaime Bulkacz¹, Kym F Faull

¹Section of Periodontics, UCLA School of Dentistry, USA. Jbulkacz@ucla.edu

|January 20, 2009

Summary

Prevotella intermedia enzymes were purified and tested for activity. The study found evidence of both phospholipase A (PL-A) and phospholipase C (PL-C) activities in the enzyme preparations.

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Area of Science:

Microbiology
Enzymology
Biochemistry

Background:

Prevotella intermedia is a bacterium found in the oral cavity.
Phospholipases are enzymes that hydrolyze phospholipids.
Understanding the enzymatic activities of Prevotella intermedia is important for studying its role in health and disease.

Purpose of the Study:

To partially purify and characterize enzyme preparations from Prevotella intermedia culture supernatants.
To investigate the presence of phospholipase activities in these preparations.

Main Methods:

Enzyme preparations were obtained from Prevotella intermedia culture supernatants.
Partial purification was achieved using ammonium sulfate precipitation and ion-exchange column chromatography.
Hydrolytic activities were assessed using (14)C-labeled phosphatidyl-choline (PC) as a substrate.
Products of hydrolysis were separated by silicic acid thin layer chromatography and quantified using liquid scintillation spectrometry.

Main Results:

Enzyme assays demonstrated linearity of substrate depletion and product formation with respect to time and protein concentration.
The identified hydrolysis products exhibited retention times consistent with lyso-phospholipids and phosphoryl-choline.
These findings strongly suggest the presence of both phospholipase A (PL-A) and phospholipase C (PL-C) activities.

Conclusions:

The study successfully identified and partially purified phospholipase activities from Prevotella intermedia.
The presence of both PL-A and PL-C activities indicates the bacterium's potential to degrade phospholipids.
Further research can explore the specific roles of these enzymes in the bacterium's biology and pathogenicity.