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Glycan shield of the ebolavirus envelope glycoprotein GP

ABSTRACT: The envelope glycoprotein GP of the ebolaviruses is essential for host cell attachment and entry. It is also the primary target of the protective and neutralizing antibody response in both natural infection and vaccination. GP is heavily glycosylated with up to 17 predicted N-linked sites, numerous O-linked glycans in its disordered mucin-like domain (MLD), and three predicted C-linked mannosylation sites. Glycosylation of GP is important for host cell attachment to cell-surface lectins, as well as GP stability and fusion activity. Moreover, it has been shown to shield GP from neutralizing activity of serum antibodies. Here, we use mass spectrometry-based glycoproteomics to profile the site-specific glycosylation patterns of ebolavirus GP, including N-, O-, and C-linked glycans.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Zaire Ebolavirus Bundibugyo Ebolavirus

SUBMITTER: Joost Snijder

LAB HEAD: Joost Snijder

PROVIDER: PXD031459 | Pride | 2022-08-02

REPOSITORIES: Pride

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			Action	DRS
	20200731_F1_Ag6_Peng0013_SA_BDBV_dTM_S2_N_alp_01.rar	Other
	20200731_F1_Ag6_Peng0013_SA_BDBV_dTM_S2_N_alp_01.raw_20220426_1139.zip	Raw
	20200731_F1_Ag6_Peng0013_SA_BDBV_dTM_S2_N_alp_02.rar	Other
	20200731_F1_Ag6_Peng0013_SA_BDBV_dTM_S2_N_alp_02.raw_20220426_1139.zip	Raw
	20200731_F1_Ag6_Peng0013_SA_BDBV_dTM_S2_N_gluc_tryp_01.rar	Other

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