Related Experiment Video
Updated: Aug 12, 2026

Analysis of the Lipid Composition of Mycobacteria by Thin Layer Chromatography
Published on: April 16, 2021
AIDS-associated mycoplasmas possess phospholipases C in the membrane
K Shibata1, T Sasaki, T Watanabe
1Department of Oral Bacteriology, Hokkaido University School of Dentistry, Sapporo, Japan.
Abstract:
Phosphatidylinositol- and phosphatidylcholine-hydrolyzing activities existed in the cell lysates of AIDS-associated Mycoplasma species, including Mycoplasma fermentans IID 812, M. fermentans incognitus, and M. penetrans GTU-54-6A1. These activities were found to be attributable to phospholipases C, because the water-soluble product from phosphatidylcholine digested by the cell lysate of M. fermentans IID 812 was phosphorylcholine. M. fermentans IID 812 was examined for localization of these enzymes, and it was found that they were associated with the membrane.
Insights
AIDS-associated Mycoplasma species possess phospholipase C enzymes that hydrolyze phosphatidylinositol and phosphatidylcholine. These enzymes, identified in Mycoplasma fermentans and Mycoplasma penetrans, are membrane-associated in M. fermentans IID 812.
Area of Science:
- Microbiology
- Enzymology
- Molecular Biology
Background:
- AIDS-associated Mycoplasma species, including Mycoplasma fermentans and Mycoplasma penetrans, are implicated in human health.
- Understanding the enzymatic activities of these Mycoplasma species is crucial for their characterization.
Purpose of the Study:
- To investigate the presence and nature of hydrolyzing activities in cell lysates of AIDS-associated Mycoplasma species.
- To identify the specific enzymes responsible for these activities and determine their localization within the cell.
Main Methods:
- Analysis of cell lysates from Mycoplasma fermentans IID 812, M. fermentans incognitus, and M. penetrans GTU-54-6A1.
- Enzymatic assays to detect phosphatidylinositol- and phosphatidylcholine-hydrolyzing activities.
- Identification of hydrolysis products to confirm enzyme identity.
- Enzyme localization studies using Mycoplasma fermentans IID 812.
Main Results:
- Phosphatidylinositol- and phosphatidylcholine-hydrolyzing activities were detected in the cell lysates of all tested AIDS-associated Mycoplasma species.
- These activities were attributed to phospholipases C, with phosphorylcholine identified as the water-soluble product of phosphatidylcholine digestion by M. fermentans IID 812.
- Enzymes responsible for these hydrolyzing activities in M. fermentans IID 812 were found to be associated with the cell membrane.
Conclusions:
- AIDS-associated Mycoplasma species possess membrane-bound phospholipase C enzymes.
- These enzymes contribute to the biochemical repertoire of Mycoplasma species relevant to AIDS.
- Further research into these enzymes may reveal their role in Mycoplasma pathogenesis or host interactions.
More Related Videos
06:04Antigen-Capture Enzyme-Linked Immunosorbent Assay for Specific Detection of Mycoplasma pneumoniae
Published on: February 24, 2023
10:31A Liposome Membrane Permeability Assay for Investigating the Effects of Phosphatidylinositol Phosphate Groups on Membranotropic Action of Venom PLA2
Published on: September 26, 2025
Related Concept Videos
Phosphoinositides and PIPs
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Anaphase Promoting Complex
Bacterial Phylum Chlamydiae
Bacterial Phylum Planctomycetes
Bacterial Phylum Tenericutes
Diversity of Protists II