Evidence map›Paper›PMID 37684364›Full record

ArticleCommunications chemistry2023

Simplifying glycan monitoring of complex antigens such as the SARS-CoV-2 spike to accelerate vaccine development.

Janelle Sauvageau, Izel Koyuturk, Frank St Michael, Denis Brochu, Marie-France Goneau, Ian Schoenhofen, Sylvie Perret, Alexandra Star, Anna Robotham, Arsalan Haqqani and 3 more

Open access · goldAbstract read
In one paragraph

Article in Communications chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 36% of its field
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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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

13 authors at 1 institution in 1 country.

Janelle SauvageauHuman Health Therapeutics Research Centre, National Research Council of Canada, 100 Sussex Dr., Ottawa, ON, K1A 0R6, Canada. Janelle.Sauvageau@nrc-cnrc.gc.ca.ORCID http://orcid.org/0000-0001-7476-8424
Izel KoyuturkDepartment of Biochemistry and Molecular Medicine, Faculty of Medicine, Université de Montréal, Montréal, H3C 3J7, Canada.
Frank St MichaelHuman Health Therapeutics Research Centre, National Research Council of Canada, 100 Sussex Dr., Ottawa, ON, K1A 0R6, Canada.
Denis BrochuHuman Health Therapeutics Research Centre, National Research Council of Canada, 100 Sussex Dr., Ottawa, ON, K1A 0R6, Canada.
Marie-France GoneauHuman Health Therapeutics Research Centre, National Research Council of Canada, 100 Sussex Dr., Ottawa, ON, K1A 0R6, Canada.
Ian SchoenhofenHuman Health Therapeutics Research Centre, National Research Council of Canada, 100 Sussex Dr., Ottawa, ON, K1A 0R6, Canada.
Sylvie PerretHuman Health Therapeutics Research Centre, National Research Council of Canada, 6100 Avenue Royalmount, Montréal, QC, H4P 2R2, Canada.
Alexandra StarHuman Health Therapeutics Research Centre, National Research Council of Canada, 100 Sussex Dr., Ottawa, ON, K1A 0R6, Canada.ORCID http://orcid.org/0000-0001-9524-4312
Anna RobothamHuman Health Therapeutics Research Centre, National Research Council of Canada, 100 Sussex Dr., Ottawa, ON, K1A 0R6, Canada.
Arsalan HaqqaniHuman Health Therapeutics Research Centre, National Research Council of Canada, 100 Sussex Dr., Ottawa, ON, K1A 0R6, Canada.
John KellyHuman Health Therapeutics Research Centre, National Research Council of Canada, 100 Sussex Dr., Ottawa, ON, K1A 0R6, Canada.
Michel GilbertHuman Health Therapeutics Research Centre, National Research Council of Canada, 100 Sussex Dr., Ottawa, ON, K1A 0R6, Canada.
Yves DurocherDepartment of Biochemistry and Molecular Medicine, Faculty of Medicine, Université de Montréal, Montréal, H3C 3J7, Canada.
National Research Council Canada · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosylation is a key quality attribute that must be closely monitored for protein therapeutics. Established assays such as HILIC-Fld of released glycans and LC-MS of glycopeptides work well for glycoproteins with a few glycosylation sites but are less amenable for those with multiple glycosylation sites, resulting in complex datasets that are time consuming to generate and difficult to analyze. As part of efforts to improve preparedness for future pandemics, researchers are currently assessing where time can be saved in the vaccine development and production process. In this context, we evaluated if neutral and acidic monosaccharides analysis via HPAEC-PAD could be used as a rapid and robust alternative to LC-MS and HILIC-Fld for monitoring glycosylation between protein production batches. Using glycoengineered spike proteins we show that the HPAEC-PAD monosaccharide assays could quickly and reproducibly detect both major and minor glycosylation differences between batches. Moreover, the monosaccharide results aligned well with those obtained by HILIC-Fld and LC-MS.

Identifiers

PMID37684364
PMCPMC10491790
OpenAlexW4386560682

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.