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<p><i>Mycoplasma pneumoniae (MPN) i</i>s a bacterial pathogen that primarily causes atypical pneumonia. It cannot synthesize certain essential lipids and therefore relies on the host for their acquisition to survive. <i>MPN</i> has been detected in increased amounts within ruptured atherosclerotic plaques. In this work, we show that the protein P116 facilitates cholesterol acquisition from LDL, HDL and various cell types. Targeting P116’s C-terminal domain with a monoclonal antibody inhibits cholesterol acquisition and bacterial growth in vitro. Phase contrast epifluorescence microscopy of human arteries reveals that this antibody blocks <i>MPN</i> binding to atherosclerotic lesions ex vivo. Additionally, an <i>MPN</i> chassis injected into hyperlipidemic female mice localizes to the liver and atherosclerotic plaques. Here, we report that P116 plays a role in extracting essential lipids from lipoproteins and host cells and regulates <i>MPN</i> localization to atheromatous plaques. The study highlights <i>MPN</i>’s potential as a tool for targeting atherosclerotic lesions and fatty liver.</p>

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Sources of essential lipids for Mycoplasma pneumoniae via P116 to target liver and atherosclerotic lesions

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年12月16日

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  • David Vizarraga,
  • Marina Marcos,
  • Noemi Rotllan,
  • Jesús Martín,
  • David Santos,
  • Mercedes Camacho,
  • Begoña Soto,
  • Lorena Velasco-Reniu,
  • Pablo Guerra,
  • Félix Pareja,
  • María Collantes,
  • Wanlu Wu,
  • Irene Rodríguez-Arce,
  • Luis Serrano,
  • Jaume Piñol,
  • Ignacio Fita,
  • Joan Carles Escolà-Gil

摘要

Mycoplasma pneumoniae (MPN) is a bacterial pathogen that primarily causes atypical pneumonia. It cannot synthesize certain essential lipids and therefore relies on the host for their acquisition to survive. MPN has been detected in increased amounts within ruptured atherosclerotic plaques. In this work, we show that the protein P116 facilitates cholesterol acquisition from LDL, HDL and various cell types. Targeting P116’s C-terminal domain with a monoclonal antibody inhibits cholesterol acquisition and bacterial growth in vitro. Phase contrast epifluorescence microscopy of human arteries reveals that this antibody blocks MPN binding to atherosclerotic lesions ex vivo. Additionally, an MPN chassis injected into hyperlipidemic female mice localizes to the liver and atherosclerotic plaques. Here, we report that P116 plays a role in extracting essential lipids from lipoproteins and host cells and regulates MPN localization to atheromatous plaques. The study highlights MPN’s potential as a tool for targeting atherosclerotic lesions and fatty liver.