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_2
Snippet: Several roles have been attributed to glycans attached to viral glycoproteins. Glycans can serve as ligands for Ca 2Ï© -dependent (C-type) lectins (CLECs), facilitating viral attachment and internalization in a variety of cell types (10) . Additionally, glycans promote protein folding/stability and virion incorporation of GP, as demonstrated in studies with Newcastle disease virus and Lassa virus (11, 12) . In the case of Nipah virus G/F proteins.....
Document: Several roles have been attributed to glycans attached to viral glycoproteins. Glycans can serve as ligands for Ca 2Ï© -dependent (C-type) lectins (CLECs), facilitating viral attachment and internalization in a variety of cell types (10) . Additionally, glycans promote protein folding/stability and virion incorporation of GP, as demonstrated in studies with Newcastle disease virus and Lassa virus (11, 12) . In the case of Nipah virus G/F proteins, not only does glycosylation help protein expression, it also decreases membrane fusion efficiency, thereby controlling premature fusion events (13, 14) . Furthermore, the glycans on human immunodeficiency virus (HIV) gp120/gp41, Nipah virus G/F, hepatitis C virus E1/E2, and influenza A virus hemagglutinin (HA) protect virions from antibody-mediated neutralization (15) . Despite the high degree of glycosylation found on filovirus GPs, the importance of the N-linked glycans on EBOV GP1 to the structure and function of the protein has not been well studied. Here, we assess the structural and functional importance of N-linked glycans on EBOV GP1.
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