HIV envelope antigen valency on peptide nanofibers modulates antibody magnitude and binding breadth

Abstract A major challenge in developing an effective vaccine against HIV-1 is the genetic diversity of its viral envelope. Because of the broad range of sequences exhibited by HIV-1 strains, protective antibodies must be able to bind and neutralize a widely mutated viral envelope protein. No vaccin...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Chelsea N. Fries, Jui-Lin Chen, Maria L. Dennis, Nicole L. Votaw, Joshua Eudailey, Brian E. Watts, Kelly M. Hainline, Derek W. Cain, Richard Barfield, Cliburn Chan, M. Anthony Moody, Barton F. Haynes, Kevin O. Saunders, Sallie R. Permar, Genevieve G. Fouda, Joel H. Collier
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
Materias:
R
Q
Acceso en línea:https://doaj.org/article/9b1d282b3398438e8effddf57c228cf2
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:9b1d282b3398438e8effddf57c228cf2
record_format dspace
spelling oai:doaj.org-article:9b1d282b3398438e8effddf57c228cf22021-12-02T18:30:45ZHIV envelope antigen valency on peptide nanofibers modulates antibody magnitude and binding breadth10.1038/s41598-021-93702-x2045-2322https://doaj.org/article/9b1d282b3398438e8effddf57c228cf22021-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-93702-xhttps://doaj.org/toc/2045-2322Abstract A major challenge in developing an effective vaccine against HIV-1 is the genetic diversity of its viral envelope. Because of the broad range of sequences exhibited by HIV-1 strains, protective antibodies must be able to bind and neutralize a widely mutated viral envelope protein. No vaccine has yet been designed which induces broadly neutralizing or protective immune responses against HIV in humans. Nanomaterial-based vaccines have shown the ability to generate antibody and cellular immune responses of increased breadth and neutralization potency. Thus, we have developed supramolecular nanofiber-based immunogens bearing the HIV gp120 envelope glycoprotein. These immunogens generated antibody responses that had increased magnitude and binding breadth compared to soluble gp120. By varying gp120 density on nanofibers, we determined that increased antigen valency was associated with increased antibody magnitude and germinal center responses. This study presents a proof-of-concept for a nanofiber vaccine platform generating broad, high binding antibody responses against the HIV-1 envelope glycoprotein.Chelsea N. FriesJui-Lin ChenMaria L. DennisNicole L. VotawJoshua EudaileyBrian E. WattsKelly M. HainlineDerek W. CainRichard BarfieldCliburn ChanM. Anthony MoodyBarton F. HaynesKevin O. SaundersSallie R. PermarGenevieve G. FoudaJoel H. CollierNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-15 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Chelsea N. Fries
Jui-Lin Chen
Maria L. Dennis
Nicole L. Votaw
Joshua Eudailey
Brian E. Watts
Kelly M. Hainline
Derek W. Cain
Richard Barfield
Cliburn Chan
M. Anthony Moody
Barton F. Haynes
Kevin O. Saunders
Sallie R. Permar
Genevieve G. Fouda
Joel H. Collier
HIV envelope antigen valency on peptide nanofibers modulates antibody magnitude and binding breadth
description Abstract A major challenge in developing an effective vaccine against HIV-1 is the genetic diversity of its viral envelope. Because of the broad range of sequences exhibited by HIV-1 strains, protective antibodies must be able to bind and neutralize a widely mutated viral envelope protein. No vaccine has yet been designed which induces broadly neutralizing or protective immune responses against HIV in humans. Nanomaterial-based vaccines have shown the ability to generate antibody and cellular immune responses of increased breadth and neutralization potency. Thus, we have developed supramolecular nanofiber-based immunogens bearing the HIV gp120 envelope glycoprotein. These immunogens generated antibody responses that had increased magnitude and binding breadth compared to soluble gp120. By varying gp120 density on nanofibers, we determined that increased antigen valency was associated with increased antibody magnitude and germinal center responses. This study presents a proof-of-concept for a nanofiber vaccine platform generating broad, high binding antibody responses against the HIV-1 envelope glycoprotein.
format article
author Chelsea N. Fries
Jui-Lin Chen
Maria L. Dennis
Nicole L. Votaw
Joshua Eudailey
Brian E. Watts
Kelly M. Hainline
Derek W. Cain
Richard Barfield
Cliburn Chan
M. Anthony Moody
Barton F. Haynes
Kevin O. Saunders
Sallie R. Permar
Genevieve G. Fouda
Joel H. Collier
author_facet Chelsea N. Fries
Jui-Lin Chen
Maria L. Dennis
Nicole L. Votaw
Joshua Eudailey
Brian E. Watts
Kelly M. Hainline
Derek W. Cain
Richard Barfield
Cliburn Chan
M. Anthony Moody
Barton F. Haynes
Kevin O. Saunders
Sallie R. Permar
Genevieve G. Fouda
Joel H. Collier
author_sort Chelsea N. Fries
title HIV envelope antigen valency on peptide nanofibers modulates antibody magnitude and binding breadth
title_short HIV envelope antigen valency on peptide nanofibers modulates antibody magnitude and binding breadth
title_full HIV envelope antigen valency on peptide nanofibers modulates antibody magnitude and binding breadth
title_fullStr HIV envelope antigen valency on peptide nanofibers modulates antibody magnitude and binding breadth
title_full_unstemmed HIV envelope antigen valency on peptide nanofibers modulates antibody magnitude and binding breadth
title_sort hiv envelope antigen valency on peptide nanofibers modulates antibody magnitude and binding breadth
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/9b1d282b3398438e8effddf57c228cf2
work_keys_str_mv AT chelseanfries hivenvelopeantigenvalencyonpeptidenanofibersmodulatesantibodymagnitudeandbindingbreadth
AT juilinchen hivenvelopeantigenvalencyonpeptidenanofibersmodulatesantibodymagnitudeandbindingbreadth
AT marialdennis hivenvelopeantigenvalencyonpeptidenanofibersmodulatesantibodymagnitudeandbindingbreadth
AT nicolelvotaw hivenvelopeantigenvalencyonpeptidenanofibersmodulatesantibodymagnitudeandbindingbreadth
AT joshuaeudailey hivenvelopeantigenvalencyonpeptidenanofibersmodulatesantibodymagnitudeandbindingbreadth
AT brianewatts hivenvelopeantigenvalencyonpeptidenanofibersmodulatesantibodymagnitudeandbindingbreadth
AT kellymhainline hivenvelopeantigenvalencyonpeptidenanofibersmodulatesantibodymagnitudeandbindingbreadth
AT derekwcain hivenvelopeantigenvalencyonpeptidenanofibersmodulatesantibodymagnitudeandbindingbreadth
AT richardbarfield hivenvelopeantigenvalencyonpeptidenanofibersmodulatesantibodymagnitudeandbindingbreadth
AT cliburnchan hivenvelopeantigenvalencyonpeptidenanofibersmodulatesantibodymagnitudeandbindingbreadth
AT manthonymoody hivenvelopeantigenvalencyonpeptidenanofibersmodulatesantibodymagnitudeandbindingbreadth
AT bartonfhaynes hivenvelopeantigenvalencyonpeptidenanofibersmodulatesantibodymagnitudeandbindingbreadth
AT kevinosaunders hivenvelopeantigenvalencyonpeptidenanofibersmodulatesantibodymagnitudeandbindingbreadth
AT sallierpermar hivenvelopeantigenvalencyonpeptidenanofibersmodulatesantibodymagnitudeandbindingbreadth
AT genevievegfouda hivenvelopeantigenvalencyonpeptidenanofibersmodulatesantibodymagnitudeandbindingbreadth
AT joelhcollier hivenvelopeantigenvalencyonpeptidenanofibersmodulatesantibodymagnitudeandbindingbreadth
_version_ 1718377995487412224