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Updated: May 21, 2025

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
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Rab11 Binding Promotes the p14 FAST Protein-Induced Syncytium Formation

Shuru Lin1,2, Zhengfei Qi3,4,2, Quanxiang Yu2

  • 1College of Chinese Medicine, Guangzhou University of Chinese Medicine, Guangzhou 510006, China.

ACS Omega
|May 19, 2025
PubMed

Insights

Reptile reoviruses

Area of Science:

  • Virology
  • Cell Biology
  • Molecular Biology

Background:

  • Reptile reoviruses utilize the p14 fusion-associated small transmembrane (FAST) protein for cell-cell membrane fusion.
  • The p14 protein is synthesized and trafficked to the plasma membrane via the endoplasmic reticulum-Golgi pathway.
  • A polybasic motif (PBM) in the p14 cytosolic endodomain interacts with Rab11 on the Golgi.

Purpose of the Study:

  • To investigate the interaction between the p14 FAST protein and Rab11.
  • To elucidate the role of Rab11 in p14-mediated membrane fusion.
  • To explore the potential of p14 as a fusion peptide.

Main Methods:

  • Surface plasmon resonance (SPR) was employed to assess the binding affinity between p141-69 and Rab11.
  • Cellular assays were conducted to evaluate the impact of Rab11 on p14-induced syncytium formation and membrane fusion efficiency.
  • Preliminary experiments explored p141-69's ability to induce liposome-cell fusion.

Main Results:

  • SPR confirmed a significant binding affinity between p141-69 and Rab11.
  • Rab11 was demonstrated to directly enhance p14-induced syncytium formation and improve membrane fusion efficiency at the cellular level.
  • Preliminary data suggests p141-69 can function as a fusion peptide, triggering liposome-cell fusion.

Conclusions:

  • Rab11 plays a direct and crucial role in facilitating p14 FAST protein-mediated membrane fusion.
  • The interaction between p14 and Rab11 is essential for efficient viral entry and cell-cell fusion.
  • p141-69 shows potential as a fusion peptide for applications in membrane fusion studies.

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