Evidence map›Paper›PMID 33657316›Full record

ArticleJournal of the American Chemical Society2021

Heterogeneity of Glycan Processing on Trimeric SARS-CoV-2 Spike Protein Revealed by Charge Detection Mass Spectrometry.

Lohra M Miller, Lauren F Barnes, Shannon A Raab, Benjamin E Draper, Tarick J El-Baba, Corinne A Lutomski, Carol V Robinson, David E Clemmer, Martin F Jarrold

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

34 citing papers in PubMed.

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  15. Uncovering the Role ofJournal of the American Chemical Society · 2023
    Article
  16. Dissecting the structural heterogeneity of proteins by native mass spectrometry.Protein science : a publication of the Protein Society · 2023
    Review
  17. Article
  18. Review
  19. Review
  20. Characterization of a SARS-CoV-2 spike protein reference material.Analytical and bioanalytical chemistry · 2022
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Lohra M MillerChemistry Department, Indiana University, 800 E Kirkwood Ave, Bloomington Indiana 47405, United States.
Lauren F BarnesChemistry Department, Indiana University, 800 E Kirkwood Ave, Bloomington Indiana 47405, United States.
Shannon A RaabChemistry Department, Indiana University, 800 E Kirkwood Ave, Bloomington Indiana 47405, United States.
Benjamin E DraperMegadalton Solutions, 3520 E Bluebird Ln, Bloomington Indiana 47401, United States.
Tarick J El-BabaDepartment of Chemistry, University of Oxford, South Parks Road, Oxford, OXI 3QZ, U.K.
Corinne A LutomskiDepartment of Chemistry, University of Oxford, South Parks Road, Oxford, OXI 3QZ, U.K.ORCID 0000-0001-7509-103X
Carol V RobinsonDepartment of Chemistry, University of Oxford, South Parks Road, Oxford, OXI 3QZ, U.K.ORCID 0000-0001-7829-5505
David E ClemmerChemistry Department, Indiana University, 800 E Kirkwood Ave, Bloomington Indiana 47405, United States.ORCID 0000-0003-4039-1360
Martin F JarroldChemistry Department, Indiana University, 800 E Kirkwood Ave, Bloomington Indiana 47405, United States.ORCID 0000-0001-7084-176X

Funding

Developing High-Resolution Ion Mobility Spectrometry-Charge Detection-Mass Spectrometry for Rapid Analysis in the Megadalton to Gigadalton RegimeR01GM131100 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI CLEMMER, DAVID E., JARROLD, MARTIN F · 2019 to 2022
$2.1M
Development of high resolution mobility measurements for structural biologyR01GM121751 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI CLEMMER, DAVID E., LAGANOWSKY, ARTHUR D · 2017 to 2020
$1.7M
Medical Research Council MR/N020413/1NIGMS NIH HHS R01 GM121751NIGMS NIH HHS R01 GM131100Wellcome Trust
6 · The paper itself

Abstract

The heterogeneity associated with glycosylation of the 66 N-glycan sites on the protein trimer making up the spike (S) region of the SARS-CoV-2 virus has been assessed by charge detection mass spectrometry (CDMS). CDMS allows simultaneous measurement of the mass-to-charge ratio and charge of individual ions, so that mass distributions can be determined for highly heterogeneous proteins such as the heavily glycosylated S protein trimer. The CDMS results are compared to recent glycoproteomics studies of the structure and abundance of glycans at specific sites. Interestingly, average glycan masses determined by "top-down" CDMS measurements are 35-47% larger than those obtained from the "bottom-up" glycoproteomics studies, suggesting that the glycoproteomic measurements underestimated the abundances of larger, more-complex glycans. Moreover, the distribution of glycan masses determined by CDMS is much broader than the distribution expected from the glycoproteomics studies, assuming that glycan processing on each trimer is not correlated. The breadth of the glycan mass distribution therefore indicates heterogeneity in the extent of glycan processing of the S protein trimers, with some trimers being much more heavily processed than others. This heterogeneity may have evolved as a way of further confounding the host's immune system.

Indexed as

Mass SpectrometryProtein MultimerizationProtein Structure, QuaternaryHEK293 CellsHumansPolysaccharidesProtein DomainsSpike Glycoprotein, CoronavirusPolysaccharidesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID33657316
PMCPMC8543487

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.