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PMID:19553334
| Citation |
Whitman, SD, Smith, EC and Dutch, RE (2009) Differential rates of protein folding and cellular trafficking for the Hendra virus F and G proteins: implications for F-G complex formation. J. Virol. 83:8998-9001 |
|---|---|
| Abstract |
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. |
| Links |
PubMed PMC2738157 Online version:10.1128/JVI.00414-09 |
| Keywords |
Animals; Cercopithecus aethiops; Endoplasmic Reticulum/chemistry; Hendra Virus/physiology; Protein Folding; Protein Multimerization; Protein Transport; Vero Cells; Viral Envelope Proteins/metabolism; Viral Fusion Proteins/metabolism |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0044228: host cell surface |
ECO:0000314: |
C |
Figure 3 is showing the trafficking rates of Hendra virus G/glycoprotein G/Hendra G as it makes its way to the surface of the cell in Henipavirus Hendra. |
complete | ||||
| GO:0044228: host cell surface |
ECO:0000314: |
C |
Figure 3 is showing the trafficking rates of Hendra virus F/fusion glycoprotein F0/Hendra F0 as it makes its way to the surface of the cell in Henipavirus Hendra. |
complete | ||||
Notes
See also
References
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