Evidence map›Paper›PMID 37972669›Full record

ReviewBiotechnology advances

Influence of glycosylation on the immunogenicity and antigenicity of viral immunogens.

Maddy L Newby, Joel D Allen, Max Crispin

Open access · hybridAbstract readReview
In one paragraph

Review in Biotechnology advances. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

30 citing papers in PubMed, 41 citations in OpenAlex.

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  14. Molecular Surveillance, Evolution, and Vaccine Strain Match of theInternational journal of molecular sciences · 2026
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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

3 authors at 1 institution in 1 country.

Maddy L NewbySchool of Biological Sciences, University of Southampton, Southampton, SO17 1BJ, UK.
Joel D AllenSchool of Biological Sciences, University of Southampton, Southampton, SO17 1BJ, UK. Electronic address: joel.allen@soton.ac.uk.
Max CrispinSchool of Biological Sciences, University of Southampton, Southampton, SO17 1BJ, UK. Electronic address: max.crispin@soton.ac.uk.
University of Southampton · GB

Funding

Identification of neutralizing epitopes on SARS-CoV-2 spike for design of vaccines and small-molecule antiviralsUM1AI144462 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI BURTON, DENNIS R. · 2019 to 2025
$201.6M
Support Component D/Vaccine Discovery, Concept to ClinicUM1AI100663 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI GODZIK, ADAM · 2012 to 2018
$131.5M
Dissecting the mechanisms of HIV resistance in vivo to broadly neutralizing antibodiesU01AI169587 · NIAID · UNIVERSITY OF MINNESOTA · PI Priyamvada Acharya, Brandon James DeKosky · 2022 to 2026
$7.8M
NIAID NIH HHS U01 AI169587NIAID NIH HHS UM1 AI100663NIAID NIH HHS UM1 AI144462
6 · The paper itself

Abstract

A key aspect of successful viral vaccine design is the elicitation of neutralizing antibodies targeting viral attachment and fusion glycoproteins that embellish viral particles. This observation has catalyzed the development of numerous viral glycoprotein mimetics as vaccines. Glycans can dominate the surface of viral glycoproteins and as such, the viral glycome can influence the antigenicity and immunogenicity of a candidate vaccine. In one extreme, glycans can form an integral part of epitopes targeted by neutralizing antibodies and are therefore considered to be an important feature of key immunogens within an immunization regimen. In the other extreme, the existence of peptide and bacterially expressed protein vaccines shows that viral glycosylation can be dispensable in some cases. However, native-like glycosylation can indicate native-like protein folding and the presence of conformational epitopes. Furthermore, going beyond native glycan mimicry, in either occupancy of glycosylation sites or the glycan processing state, may offer opportunities for enhancing the immunogenicity and associated protection elicited by an immunogen. Here, we review key determinants of viral glycosylation and how recombinant immunogens can recapitulate these signatures across a range of enveloped viruses, including HIV-1, Ebola virus, SARS-CoV-2, Influenza and Lassa virus. The emerging understanding of immunogen glycosylation and its control will help guide the development of future vaccines in both recombinant protein- and nucleic acid-based vaccine technologies.

Indexed as

GlycoproteinsVaccinesAntibodies, NeutralizingEpitopesGlycosylationPolysaccharidesAntibodies, NeutralizingEpitopesGlycoproteinsPolysaccharidesVaccinesGlycoproteinGlycosylationImmunogenVaccineVirus

Identifiers

PMID37972669
PMCPMC10867814
OpenAlexW4388665827

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.