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Updated: Jun 18, 2026
Enrichment of Bacterial Lipoproteins and Preparation of N-terminal Lipopeptides for Structural Determination by Mass Spectrometry
Published on: May 21, 2018
Essential protein P116 extracts cholesterol and other indispensable lipids for Mycoplasmas
Lasse Sprankel1, David Vizarraga2, Jesús Martín2
1Buchmann Institute for Molecular Life Sciences and Institute of Biophysics, Goethe University Frankfurt, Frankfurt, Germany.
Abstract:
Mycoplasma pneumoniae, responsible for approximately 30% of community-acquired human pneumonia, needs to extract lipids from the host environment for survival and proliferation. Here, we report a comprehensive structural and functional analysis of the previously uncharacterized protein P116 (MPN_213). Single-particle cryo-electron microscopy of P116 reveals a homodimer presenting a previously unseen fold, forming a huge hydrophobic cavity, which is fully accessible to solvent. Lipidomics analysis shows that P116 specifically extracts lipids such as phosphatidylcholine, sphingomyelin and cholesterol. Structures of different conformational states reveal the mechanism by which lipids are extracted. This finding immediately suggests a way to control Mycoplasma infection by interfering with lipid uptake.
Insights
Mycoplasma pneumoniae uses protein P116 to extract essential lipids from host cells. Targeting this lipid uptake mechanism offers a novel strategy to control pneumonia infections.
Area of Science:
- Microbiology and Structural Biology
Background:
- Mycoplasma pneumoniae causes significant community-acquired pneumonia.
- This bacterium requires host lipids for survival and proliferation.
Purpose of the Study:
- To characterize the structure and function of the uncharacterized protein P116 (MPN_213) in Mycoplasma pneumoniae.
- To elucidate the mechanism of lipid extraction by P116.
Main Methods:
- Single-particle cryo-electron microscopy was used to determine the structure of P116.
- Lipidomics analysis identified specific lipids extracted by P116.
- Structural analysis of conformational states revealed the lipid extraction mechanism.
Main Results:
- P116 forms a homodimer with a unique fold and a large, solvent-accessible hydrophobic cavity.
- P116 specifically extracts phosphatidylcholine, sphingomyelin, and cholesterol.
- Conformational changes in P116 facilitate lipid extraction.
Conclusions:
- Protein P116 plays a crucial role in Mycoplasma pneumoniae lipid acquisition.
- Interfering with P116-mediated lipid uptake presents a potential therapeutic strategy against Mycoplasma infections.
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