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Glycan shield of the ebolavirus envelope glycoprotein GP

Peng, Weiwei and Rayaprolu, Vamseedhar and Parvate, Amar D. and Pronker, Matti F. and Hui, Sean and Parekh, Diptiben and Shaffer, Kelly and Yu, Xiaoying and Saphire, Erica O. and Snijder, Joost (2022) Glycan shield of the ebolavirus envelope glycoprotein GP. Communications Biology, 5 . Art. No. 785. ISSN 2399-3642. PMCID PMC9352669. doi:10.1038/s42003-022-03767-1.

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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.

Item Type:Article
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URLURL TypeDescription Paper CentralArticle
Peng, Weiwei0000-0003-0195-2786
Rayaprolu, Vamseedhar0000-0002-2823-2984
Parvate, Amar D.0000-0001-9282-5015
Pronker, Matti F.0000-0001-5268-7690
Hui, Sean0000-0002-9870-6823
Parekh, Diptiben0000-0002-1972-9462
Shaffer, Kelly0000-0002-6212-1428
Yu, Xiaoying0000-0002-6778-5004
Saphire, Erica O.0000-0002-1206-7451
Snijder, Joost0000-0002-9310-8226
Additional Information:© The Author(s) 2022. Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit Received 28 June 2022; Accepted 25 July 2022; Published 04 August 2022. The authors would like to thank everyone in the Biomolecular Mass Spectrometry and Proteomics group at Utrecht University for support and helpful discussions. This research was funded by the Dutch Research Council NWO Gravitation 2013 BOO, Institute for Chemical Immunology (ICI; 024.002.009) to J.S., and NIAID U19 AI142790 to E.O.S. Data availability: The raw LC-MS/MS files and glycopeptide identifications have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository with the dataset identifier PXD031459. All reagents and relevant data are available from the authors upon request. Contributions: W.P., E.O.S. and J.S. conceived of the project. W.P. performed all glycoproteomics experiments. W.P. and J.S. analyzed the glycoproteomics data. V.R., A.D.P., S.H., D.P, K.S. and X.Y produced the GP samples. M.F.P. modelled the C-mannosylation. All authors contributed to interpretation of the results and wrote the manuscript. E.O.S and J.S. acquired funding. The authors declare no competing interests. Peer review information: Primary Handling Editor: Gene Chong.
Funding AgencyGrant Number
Nederlandse Organisatie voor Wetenschappelijk Onderzoek (NWO)ICI; 024.002.009
NIHU19 AI142790
PubMed Central ID:PMC9352669
Record Number:CaltechAUTHORS:20220208-948157000
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Official Citation:Peng, W., Rayaprolu, V., Parvate, A.D. et al. Glycan shield of the ebolavirus envelope glycoprotein GP. Commun Biol 5, 785 (2022).
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:113330
Deposited By: George Porter
Deposited On:08 Feb 2022 20:47
Last Modified:17 Aug 2022 16:38

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