Differential rates of protein folding and cellular trafficking for the Hendra virus F and G proteins: implications for F-G complex formation.
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.
Whitman
Shannon D
SD
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.
Smith
Everett Clinton
EC
Dutch
Rebecca Ellis
RE
D000818:Animals; D002522:Chlorocebus aethiops; D004721:Endoplasmic Reticulum / Q000737:chemistry; D045404:Hendra Virus / Q000502:physiology*; D017510:Protein Folding; D055503:Protein Multimerization; D021381:Protein Transport; D014709:Vero Cells; D014759:Viral Envelope Proteins / Q000378:metabolism*; D014760:Viral Fusion Proteins / Q000378:metabolism*
D014759:Viral Envelope Proteins; D014760:Viral Fusion Proteins; C116204:attachment protein G