期刊
JOURNAL OF VIROLOGY
卷 83, 期 17, 页码 8998-9001出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.00414-09
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- NIAID [A151517]
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI051517] Funding Source: NIH RePORTER
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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