Skip to main content
Molecular & Cellular Proteomics

Main menu

  • Home
  • Articles
    • Current Issue
    • Papers in Press
    • Reviews and Minireviews
    • Special Issues
    • Editorials
    • Archive
    • Letters to the Editor (eLetters)
  • Info for
    • Authors
      • Editorial Policies
      • How to Submit
      • Manuscript Contents & Organization
      • Data Reporting Requirements
      • Publication Charges
    • Reviewers
    • Librarians
    • Advertisers
    • Subscribers
  • Guidelines
    • Proteomic Identification
      • Checklist (PDF)
      • Instructions for Annotated Spectra
      • Tutorial (PDF)
    • Clinical Proteomics
      • Checklist (PDF)
    • Glycomic Identification
      • Checklist (PDF)
    • Targeted Proteomics
      • Checklist (PDF)
    • Data-Independent Acquisition
      • Checklist (PDF)
    • Frequently Asked Questions
  • About
    • Mission Statement and Scope
    • Editorial Policies
    • Editorial Board
    • MCP Lectureships
    • Permissions and Licensing
    • Partners
    • Alerts
    • Contact Us

Submit

  • Submit
  • Publications
    • ASBMB
    • Molecular & Cellular Proteomics
    • Journal of Biological Chemistry
    • Journal of Lipid Research

User menu

  • Register
  • Subscribe
  • My alerts
  • Log in
  • My Cart

Search

  • Advanced search
  • Publications
    • ASBMB
    • Molecular & Cellular Proteomics
    • Journal of Biological Chemistry
    • Journal of Lipid Research
  • Register
  • Subscribe
  • My alerts
  • Log in
  • My Cart
Molecular & Cellular Proteomics

Advanced Search

  • Home
  • Articles
    • Current Issue
    • Papers in Press
    • Reviews and Minireviews
    • Special Issues
    • Editorials
    • Archive
    • Letters to the Editor (eLetters)
  • Info for
    • Authors
      • Editorial Policies
      • How to Submit
      • Manuscript Contents & Organization
      • Data Reporting Requirements
      • Publication Charges
    • Reviewers
    • Librarians
    • Advertisers
    • Subscribers
  • Guidelines
    • Proteomic Identification
      • Checklist (PDF)
      • Instructions for Annotated Spectra
      • Tutorial (PDF)
    • Clinical Proteomics
      • Checklist (PDF)
    • Glycomic Identification
      • Checklist (PDF)
    • Targeted Proteomics
      • Checklist (PDF)
    • Data-Independent Acquisition
      • Checklist (PDF)
    • Frequently Asked Questions
  • About
    • Mission Statement and Scope
    • Editorial Policies
    • Editorial Board
    • MCP Lectureships
    • Permissions and Licensing
    • Partners
    • Alerts
    • Contact Us
  • Submit
Review

Why Glycosylation Matters in Building a Better Flu Vaccine

Deborah Chang and View ORCID ProfileJoseph Zaia  Correspondence email
Molecular & Cellular Proteomics December 1, 2019, First published on October 11, 2019, 18 (12) 2348-2358; https://doi.org/10.1074/mcp.R119.001491
Deborah Chang
Dept. of Biochemistry, Boston University School of Medicine, Boston, MA 02118
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Joseph Zaia
Dept. of Biochemistry, Boston University School of Medicine, Boston, MA 02118
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Joseph Zaia
  • For correspondence: jzaia@bu.edu
  • Article
  • Figures & Data
  • Info & Metrics
  • eLetters
  • PDF
Loading

This article requires a subscription to view the full text. If you have a subscription you may use the login form below to view the article. Access to this article can also be purchased.

Graphical Abstract

Figure1
  • Download figure
  • Open in new tab
  • Download powerpoint

Highlights

  • Glycosylation is not currently considered in flu vaccine design.

  • Glycosylation influences on immunodominance are not well understood.

  • Identification of site-specific glycosylation using mass spectrometry has matured.

  • New methods are needed to quantify site-specific glycosylation for vaccine design.

Abstract

Low vaccine efficacy against seasonal influenza A virus (IAV) stems from the ability of the virus to evade existing immunity while maintaining fitness. Although most potent neutralizing antibodies bind antigenic sites on the globular head domain of the IAV envelope glycoprotein hemagglutinin (HA), the error-prone IAV polymerase enables rapid evolution of key antigenic sites, resulting in immune escape. Significantly, the appearance of new N-glycosylation consensus sequences (sequons, NXT/NXS, rarely NXC) on the HA globular domain occurs among the more prevalent mutations as an IAV strain undergoes antigenic drift. The appearance of new glycosylation shields underlying amino acid residues from antibody contact, tunes receptor specificity, and balances receptor avidity with virion escape, all of which help maintain viral propagation through seasonal mutations. The World Health Organization selects seasonal vaccine strains based on information from surveillance, laboratory, and clinical observations. Although the genetic sequences are known, mature glycosylated structures of circulating strains are not defined. In this review, we summarize mass spectrometric methods for quantifying site-specific glycosylation in IAV strains and compare the evolution of IAV glycosylation to that of human immunodeficiency virus. We argue that the determination of site-specific glycosylation of IAV glycoproteins would enable development of vaccines that take advantage of glycosylation-dependent mechanisms whereby virus glycoproteins are processed by antigen presenting cells.

  • Glycoproteomics
  • glycoprotein structure
  • viruses
  • glycoproteins
  • clinical proteomics
  • influenza A virus

Footnotes

  • Author contributions: D.C. and J.Z. wrote the paper.

  • ↵* This work is supported by NIH grant U01CA221234 and the Graduate Medical Sciences program at Boston University School of Medicine. No author has an actual or perceived conflict of interest with the contents of this article.

  • Received April 8, 2019.
  • Revision received August 18, 2019.
  • © 2019 Chang and Zaia.

Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.

View Full Text

Log in using your username and password

Forgot your user name or password?

Purchase access

You may purchase access to this article. This will require you to create an account if you don't already have one.
PreviousNext
Back to top
Print
Download PDF
Article Alerts
Sign In to Email Alerts with your Email Address
Email Article

Thank you for your interest in spreading the word on Molecular & Cellular Proteomics.

NOTE: We only request your email address so that the person you are recommending the page to knows that you wanted them to see it, and that it is not junk mail. We do not capture any email address.

Enter multiple addresses on separate lines or separate them with commas.
Why Glycosylation Matters in Building a Better Flu Vaccine
(Your Name) has sent you a message from Molecular & Cellular Proteomics
(Your Name) thought you would like to see the Molecular & Cellular Proteomics web site.
CAPTCHA
This question is for testing whether or not you are a human visitor and to prevent automated spam submissions.
Citation Tools
Why Glycosylation Matters in Building a Better Flu Vaccine
Deborah Chang, Joseph Zaia
Molecular & Cellular Proteomics December 1, 2019, First published on October 11, 2019, 18 (12) 2348-2358; DOI: 10.1074/mcp.R119.001491

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero

Request Permissions

Share
Why Glycosylation Matters in Building a Better Flu Vaccine
Deborah Chang, Joseph Zaia
Molecular & Cellular Proteomics December 1, 2019, First published on October 11, 2019, 18 (12) 2348-2358; DOI: 10.1074/mcp.R119.001491
del.icio.us logo Digg logo Reddit logo Twitter logo CiteULike logo Facebook logo Google logo Mendeley logo
  • Tweet Widget
  • Facebook Like
  • Google Plus One

In this issue

Molecular & Cellular Proteomics: 18 (12)
Molecular & Cellular Proteomics
Vol. 18, Issue 12
1 Dec 2019
  • Table of Contents
  • Table of Contents (PDF)
  • Cover (PDF)
  • About the Cover
  • Index by author
  • Ed Board (PDF)

View this article with LENS

Jump to section

  • Article
    • Graphical Abstract
    • Abstract
    • CONCLUSIONS
    • Footnotes
    • REFERENCES
  • Figures & Data
  • eLetters
  • Info & Metrics
  • PDF

  • Follow MCP on Twitter
  • RSS feeds
  • Email

Articles

  • Current Issue
  • Papers in Press
  • Archive

For Authors

  • Submit a Manuscript
  • Info for Authors

Guidelines

  • Proteomic Identification
  • Clinical Proteomics
  • Glycomic Identification
  • Targeted Proteomics
  • Frequently Asked Questions

About MCP

  • About the Journal
  • Permissions and Licensing
  • Advertisers
  • Subscribers

ASBMB Publications

  • Molecular & Cellular Proteomics
  • Journal of Biological Chemistry
  • Journal of Lipid Research
  • ASBMB Today

© 2019 American Society for Biochemistry and Molecular Biology | Privacy Policy

MCP Print ISSN 1535-9476 Online ISSN 1535-9484

Powered by HighWire