Designs of Antigen Structure and Composition for Improved Protein-Based Vaccine Efficacy

dc.contributor.authorSaylor, Kyleen
dc.contributor.authorGillam, Francisen
dc.contributor.authorLohneis, Tayloren
dc.contributor.authorZhang, Chenmingen
dc.date.accessioned2020-05-15T15:02:42Zen
dc.date.available2020-05-15T15:02:42Zen
dc.date.issued2020-02-24en
dc.description.abstractToday, vaccinologists have come to understand that the hallmark of any protective immune response is the antigen. However, it is not the whole antigen that dictates the immune response, but rather the various parts comprising the whole that are capable of influencing immunogenicity. Protein-based antigens hold particular importance within this structural approach to understanding immunity because, though different molecules can serve as antigens, only proteins are capable of inducing both cellular and humoral immunity. This fact, coupled with the versatility and customizability of proteins when considering vaccine design applications, makes protein-based vaccines (PBVs) one of today's most promising technologies for artificially inducing immunity. In this review, we follow the development of PBV technologies through time and discuss the antigen-specific receptors that are most critical to any immune response: pattern recognition receptors, B cell receptors, and T cell receptors. Knowledge of these receptors and their ligands has become exceptionally valuable in the field of vaccinology, where today it is possible to make drastic modifications to PBV structure, from primary to quaternary, in order to promote recognition of target epitopes, potentiate vaccine immunogenicity, and prevent antigen-associated complications. Additionally, these modifications have made it possible to control immune responses by modulating stability and targeting PBV to key immune cells. Consequently, careful consideration should be given to protein structure when designing PBVs in the future in order to potentiate PBV efficacy.en
dc.description.notesThis work was partially supported by the National Institute on Drug Abuse (U01DA036850) and the American Association of Immunologists Careers in Immunology Fellowship Program, both of which provided support for KS. The authors declare that this study received funding from Smithfield Foods and Murphy-Brown LLC, which provided support for FG. The funder was not involved in the study design, collection, analysis, interpretation of data, the writing of this article or the decision to submit it for publication. The department of Biological Systems Engineering, which provided support for TL. Funds were also received from Virginia Tech Open Access Subvention Fund to cover the publication fee.en
dc.description.sponsorshipNational Institute on Drug AbuseUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute on Drug Abuse (NIDA) [U01DA036850]; American Association of Immunologists Careers in Immunology Fellowship Program; Murphy-Brown LLC; Virginia Tech Open Access Subvention Fund; Smithfield Foods; department of Biological Systems Engineeringen
dc.format.mimetypeapplication/pdfen
dc.identifier.doihttps://doi.org/10.3389/fimmu.2020.00283en
dc.identifier.issn1664-3224en
dc.identifier.other283en
dc.identifier.pmid32153587en
dc.identifier.urihttp://hdl.handle.net/10919/98401en
dc.identifier.volume11en
dc.language.isoenen
dc.rightsCreative Commons Attribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.subjectvaccineen
dc.subjectimmunityen
dc.subjectantigenen
dc.subjectepitopeen
dc.subjectmodificationen
dc.subjectvaccine compositionen
dc.subjectvaccine structureen
dc.titleDesigns of Antigen Structure and Composition for Improved Protein-Based Vaccine Efficacyen
dc.title.serialFrontiers in Immunologyen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten
dc.type.dcmitypeStillImageen

Files

Original bundle
Now showing 1 - 1 of 1
Loading...
Thumbnail Image
Name:
fimmu-11-00283.pdf
Size:
1.78 MB
Format:
Adobe Portable Document Format
Description: