| Literature DB >> 17328935 |
Shannon D Whitman1, Rebecca Ellis Dutch.
Abstract
Hendra virus, like most paramyxoviruses, requires both a fusion (F) and attachment (G) protein for promotion of cell-cell fusion. Recent studies determined that Hendra F is proteolytically processed by the cellular protease cathepsin L after endocytosis. This unique cathepsin L processing results in a small percentage of Hendra F on the cell surface. To determine how the surface densities of the two Hendra glycoproteins affect fusion promotion, we performed experiments that varied the levels of glycoproteins expressed in transfected cells. Using two different fusion assays, we found a marked increase in fusion when expression of the Hendra G protein was increased, with a 1:1 molar ratio of Hendra F:G on the cell surface resulting in optimal membrane fusion. Our results also showed that Hendra G protein levels are modulated by both more rapid protein turnover and slower protein trafficking than is seen for Hendra F.Entities:
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Year: 2007 PMID: 17328935 PMCID: PMC1952237 DOI: 10.1016/j.virol.2007.01.029
Source DB: PubMed Journal: Virology ISSN: 0042-6822 Impact factor: 3.616