Glycan shield of the ebolavirus envelope glycoprotein GP

Peng, Weiwei; Rayaprolu, Vamseedhar; Parvate, Amar D.; Pronker, Matti F.; Hui, Sean; Parekh, Diptiben; Shaffer, Kelly; Yu, Xiaoying; Saphire, Erica O.; Snijder, Joost

doi:10.1038/s42003-022-03767-1

Glycan shield of the ebolavirus envelope glycoprotein GP

Journal Article · Thu Aug 04 00:00:00 EDT 2022 · Communications Biology

DOI:https://doi.org/10.1038/s42003-022-03767-1· OSTI ID:2471571

Peng, Weiwei ^[1]; Rayaprolu, Vamseedhar ^[2]; ^[3]; ^[1]; ^[4]; Parekh, Diptiben ^[5]; ^[6]; ^[5]; ^[7]; ^[1]

Utrecht University (Netherlands)
La Jolla Institute for Immunology, CA (United States); Pacific Northwest Center for CryoEM, Portland, OR (United States)
La Jolla Institute for Immunology, CA (United States); Pacific Northwest National Laboratory (PNNL), Richland, WA (United States). Environmental Molecular Sciences Laboratory (EMSL)
La Jolla Institute for Immunology, CA (United States); Washington Univ., St. Louis, MO (United States)
La Jolla Institute for Immunology, CA (United States)
La Jolla Institute for Immunology, CA (United States); California Institute of Technology (CalTech), Pasadena, CA (United States)
La Jolla Institute for Immunology, CA (United States); Univ. of California, San Diego, CA (United States)

The envelope glycoprotein GP of the ebolaviruses is essential for host cell entry and the primary target of the host antibody response. GP is heavily glycosylated with up to 17 N-linked sites, numerous O-linked glycans in its disordered mucin-like domain (MLD), and three predicted C-linked mannosylation sites. Glycosylation is important for host cell attachment, GP stability and fusion activity, and shielding from neutralization by serum antibodies. Here, we use glycoproteomics to profile the site-specific glycosylation patterns of ebolavirus GP. We detect up to 16 unique O-linked glycosylation sites in the MLD, and two O-linked sites in the receptor-binding GP1 subunit. Multiple O-linked glycans are observed within N-linked glycosylation sequons, suggesting crosstalk between the two types of modifications. We confirmed C-mannosylation of W288 in full-length trimeric GP. We find complex glycosylation at the majority of N-linked sites, while the conserved sites N257 and especially N563 are enriched in unprocessed glycans, suggesting a role in host-cell attachment via DC-SIGN/L-SIGN. Our findings illustrate how N-, O-, and C-linked glycans together build the heterogeneous glycan shield of GP, guiding future immunological studies and functional interpretation of ebolavirus GP-antibody interactions.

View Accepted Manuscript (DOE)

Research Organization:: Pacific Northwest National Laboratory (PNNL), Richland, WA (United States)

Sponsoring Organization:: USDOE

Grant/Contract Number:: AC05-76RL01830

OSTI ID:: 2471571

Journal Information:: Communications Biology, Journal Name: Communications Biology Journal Issue: 1 Vol. 5; ISSN 2399-3642

Publisher:: Springer NatureCopyright Statement

Country of Publication:: United States

Language:: English

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