2019
DOI: 10.1074/mcp.r119.001491
|View full text |Cite
|
Sign up to set email alerts
|

Why Glycosylation Matters in Building a Better Flu Vaccine

Abstract: Immunodominant influenza A virus (IAV) antigens mutate rapidly, allowing the virus to escape host antibodies. The question remains how to design vaccines that recognize conserved but subdominant IAV antigens for broader immune protection. Glycosylation is a mechanism whereby IAV evades the innate and adaptive immune systems. However, its influence on immunodominance remains poorly understood. Although mass spectrometry methods for identifying glycopeptides are maturing, quantifying glycosylation variation amon… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1

Citation Types

0
67
1

Year Published

2020
2020
2024
2024

Publication Types

Select...
4
3
1

Relationship

0
8

Authors

Journals

citations
Cited by 68 publications
(71 citation statements)
references
References 127 publications
0
67
1
Order By: Relevance
“…Two very recent preprints reporting N-glycosylation on spike protein of SARS-CoV-2 showed different glycosylation profiles, and both reports were different from our results although all three studies utilized recombinant S protein from an HEK 293-based expression system (Watanabe, Y., Allen, J.D., et al , Zhang, Y., Zhao, W., et al 2020. This indicates the caution to be exercised in determining the glycosylation on viral antigens generated from various sources as the changes in glycosylation pattern can influence the efficacy of potential vaccine candidates (Chang, D. and Zaia, J. 2019).…”
Section: Discussioncontrasting
confidence: 82%
“…Two very recent preprints reporting N-glycosylation on spike protein of SARS-CoV-2 showed different glycosylation profiles, and both reports were different from our results although all three studies utilized recombinant S protein from an HEK 293-based expression system (Watanabe, Y., Allen, J.D., et al , Zhang, Y., Zhao, W., et al 2020. This indicates the caution to be exercised in determining the glycosylation on viral antigens generated from various sources as the changes in glycosylation pattern can influence the efficacy of potential vaccine candidates (Chang, D. and Zaia, J. 2019).…”
Section: Discussioncontrasting
confidence: 82%
“…The S protein is posited to be the main or even the only antigen on viral surfaces for priming the immune system to produce an effective response (15,18). Previous studies have revealed the structural information of the SARS-CoV-2 S protein and found the coverage of N-glycans (4, Glycosylation promotes proper glycoprotein folding; however, the glycans obstruct receptor binding and proteolytic processing during antigen presentation (15,17,23).…”
Section: Discussionmentioning
confidence: 99%
“…The HIV envelope glycoprotein gp120 is heavily decorated with the immature intermediate, high-mannose glycans. The high-density glycans surrounding HIV glycoproteins limit the accessibility of glycan biosynthetic processing enzymes, terminating the synthesis of more complex end products (17,24).…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…Anti-carbohydrate antibodies have been shown to be neutralizing in other viruses, such as HIV 75 , and therefore glycosylated peptides can offer an alternative to more traditional peptide epitopes. From the perspective of vaccine development 76 , targeting glycans as epitopes would be expected to benefit from matching the glycan microheterogeneity in the vaccine to that in the circulating virus, which requires additional consideration of the choice of cell type for vaccine production.…”
Section: Assessment Of the Impact Of Glycosylation On Antigenicitymentioning
confidence: 99%