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Journal of Virology, September 2009, p. 8998-9001, Vol. 83, No. 17
0022-538X/09/$08.00+0     doi:10.1128/JVI.00414-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

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

Shannon D. Whitman, Everett Clinton Smith, and Rebecca Ellis Dutch*

Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky 40536

Received 25 February 2009/ Accepted 5 June 2009

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.

* Corresponding author. Mailing address: Department of Molecular and Cellular Biochemistry, University of Kentucky, College of Medicine, Biomedical Biological Sciences Research Building, 741 South Limestone, Lexington, KY 40536-0509. Phone: (859) 323-1795. Fax: (859) 323-1037. E-mail: rdutc2{at}uky.edu

{triangledown} Published ahead of print on 24 June 2009.

Journal of Virology, September 2009, p. 8998-9001, Vol. 83, No. 17
0022-538X/09/$08.00+0     doi:10.1128/JVI.00414-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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