Author: Lennemann, Nicholas J.; Rhein, Bethany A.; Ndungo, Esther; Chandran, Kartik; Qiu, Xiangguo; Maury, Wendy
Title: Comprehensive Functional Analysis of N-Linked Glycans on Ebola Virus GP1 Document date: 2014_1_28
ID: 6sb3ipab_5
Snippet: Initial studies were performed to disrupt the seven NGS within the GP1 core of GP1⌬muc and GP. Reduced levels of glycosylation on mutant GPs that were pseudotyped onto VSV were apparent in immunoblots, evidenced by faster migration of the mutant proteins (see Fig. S1A in the supplemental material). The expression of WT and mutant GPs in supernatants and the transduction of Vero cells mediated by these virions are summarized in Fig. S2 . Notably.....
Document: Initial studies were performed to disrupt the seven NGS within the GP1 core of GP1⌬muc and GP. Reduced levels of glycosylation on mutant GPs that were pseudotyped onto VSV were apparent in immunoblots, evidenced by faster migration of the mutant proteins (see Fig. S1A in the supplemental material). The expression of WT and mutant GPs in supernatants and the transduction of Vero cells mediated by these virions are summarized in Fig. S2 . Notably, removing more than 3 glycans from the GP1 core significantly decreased the expression of GP1⌬muc and concomitantly reduced its transduction. However, all 7 glycan sites within the GP1 core could be removed (7G) with no effect on GP expression and a significant enhancement in transduction over that of the WT, suggesting that the MLD provides stability that allows the removal of glycans from the GP1 core ( Fig. 2A) . Furthermore, these mutant GPs were incorporated into purified virions at a rate equivalent to the incorporation of the WT (Fig. S1B) .
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