Differential Rates of Protein Folding and Cellular Trafficking for the Hendra Virus F and G Proteins: Implications for F-G Complex Formation

Department of Molecular and Cellular Biochemistry, University of Kentucky, College of Medicine, Biomedical Biological Sciences Research Building, 741 South Limestone, Lexington, KY 40536-0509, USA.
Journal of Virology (Impact Factor: 4.44). 07/2009; 83(17):8998-9001. DOI: 10.1128/JVI.00414-09
Source: PubMed


Hendra virus F protein-promoted membrane fusion requires the presence of the viral attachment protein, G. However, events
leading to the association of these glycoproteins remain unclear. Results presented here demonstrate that Hendra virus G undergoes
slower secretory pathway trafficking than is observed for Hendra virus F. This slowed trafficking is not dependent on the
G protein cytoplasmic tail, the presence of the G receptor ephrin B2, or interaction with other viral proteins. Instead, Hendra
virus G was found to undergo intrinsically slow oligomerization within the endoplasmic reticulum. These results suggest that
the critical F-G interactions occur only after the initial steps of synthesis and cellular transport.

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Available from: Everett Clinton Smith, Jun 17, 2014
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