Enhanced Fusion Pore Expansion Mediated by the Trans-Acting Endodomain of the Reovirus FAST Proteins
2009

Enhancing Cell Fusion with Reovirus FAST Proteins

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Author Information

Author(s): Deniz Top, Chris Racine, Trina Ellis, Chelsey Louise Duncan, Roy Duncan

Primary Institution: Dalhousie University

Hypothesis

The endodomains of reovirus FAST proteins enhance syncytiogenesis by functioning in trans from the cytosol.

Conclusion

The p14 endodomain of reovirus FAST proteins enhances syncytium formation by acting as a soluble enhancer that influences cellular pathways involved in membrane fusion.

Supporting Evidence

  • The p14 endodomain enhances syncytium formation significantly when co-expressed with full-length FAST proteins.
  • Endogenous generation of the p14 endodomain was confirmed in virus-infected cells.
  • The enhancing activity of the p14 endodomain is not dependent on direct interactions with the fusogen.

Takeaway

The p14 endodomain helps cells stick together and form larger cells by making it easier for their membranes to fuse.

Methodology

The study involved co-transfection of cells with plasmids expressing FAST proteins and their endodomains, followed by analysis of syncytium formation and Western blotting.

Limitations

The study primarily focuses on the p14 endodomain, and the generalizability to other FAST proteins may require further investigation.

Statistical Information

P-Value

p<0.001

Statistical Significance

p<0.001

Digital Object Identifier (DOI)

10.1371/journal.ppat.1000331

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