Comprehensive Functional Analysis of N-Linked Glycans on Ebola Virus GP1

Lennemann, Nicholas J.; Rhein, Bethany A.; Ndungo, Esther; Chandran, Kartik; Qiu, Xiangguo; Maury, Wendy

ing diversification of this region of the protein. In contrast, the glycan cap and MLD have extensive sequence diversity between the different Ebola virus species. As the names suggest, both the glycan cap and the MLD are highly glycosylated, resulting in the majority of the protein being masked by glycans (Fig. 1A) (6) . The glycan cap contains only N-linked glycan sites (NGS) and, despite generally poor sequence conservation within the glycan cap, these sites are well conserved among Ebola viruses, suggesting functional significance (Fig. 1C) . In contrast to the glycan cap, the glycosylation events found in the MLD are highly variable between the different viruses and include both N-and O-linked glycans. Despite extensive glycosylation, the MLD remains highly targeted by neutralizing antibodies (7) (8) (9) .