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U.S. Department of Health and Human Services

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Virology 2010 Jan 5;396(1):135-42

Phenylalanines at positions 88 and 159 of Ebolavirus envelope glycoprotein differentially impact envelope function.

Ou W, King H, Delisle J, Shi D, Wilson CA


The envelope glycoprotein (GP) of Ebolavirus (EBOV) mediates viral entry into host cells. Through mutagenesis, we and other groups reported that two phenylalanines at positions 88 and 159 of GP are critical for viral entry. However, it remains elusive which steps of viral entry are impaired by F88 or F159 mutations and how. In this study, we further characterized these two phenylalanines through mutagenesis and examined the impact on GP expression, function, and structure. Our data suggest that F159 plays an indirect role in viral entry by maintaining EBOV GP's overall structure. In contrast, we did not detect any evidence for conformational differences in GP with F88 mutations. The data suggest that F88 influences viral entry during a step after cathepsin processing, presumably impacting viral fusion.

Category: Journal Article
PubMed ID: #19906395 DOI: 10.1016/j.virol.2009.10.028
Includes FDA Authors from Scientific Area(s): Biologics
Entry Created: 2011-10-04 Entry Last Modified: 2012-08-29