Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

HIV broadly neutralizing antibody targets

HIV broadly neutralizing antibody targets REVIEW URRENT PINION a,b a,b,c a,b,c Constantinos Kurt Wibmer , Penny L. Moore , and Lynn Morris Purpose of review To provide an update on neutralizing antibody targets in the context of the recent HIV-1 envelope trimer structure, describe new antibody isolation technologies, and discuss the implications of these data for HIV-1 prevention and therapy. Recent findings Recent advances in B-cell technologies have dramatically expanded the number of antibodies isolated from HIV-infected donors with broadly neutralizing plasma activity. These, together with the first high-resolution crystal and cryo-electron microscopy (cryo-EM) structures of a cleaved, prefusion HIV-1 trimer, have defined new regions susceptible to neutralization. This year, three epitopes in the gp120 – gp41 interface were structurally characterized, highlighting the importance of prefusion gp41 as a target. Similar to many other broadly neutralizing antibody epitopes, these new antibodies define a target that is also highly glycan dependent. Collectively, the epitopes for broadly neutralizing antibodies now reveal a continuum of vulnerability spanning the length of the HIV-1 envelope trimer. Summary Progress in the last year has provided support for the use of rationally stabilized whole HIV-1 trimers as immunogens for eliciting antibodies to multiple epitopes. Furthermore, the increasing number of broad and http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Current Opinion in HIV and Aids Wolters Kluwer Health

HIV broadly neutralizing antibody targets

Current Opinion in HIV and Aids , Volume 10 (3) – May 1, 2015

Loading next page...
 
/lp/wolters-kluwer-health/hiv-broadly-neutralizing-antibody-targets-zi4f6k0AYN

References

References for this paper are not available at this time. We will be adding them shortly, thank you for your patience.

Copyright
Copyright © 2015 Wolters Kluwer Health, Inc. All rights reserved.
ISSN
1746-630X
eISSN
1746-6318
DOI
10.1097/COH.0000000000000153
pmid
25760932
Publisher site
See Article on Publisher Site

Abstract

REVIEW URRENT PINION a,b a,b,c a,b,c Constantinos Kurt Wibmer , Penny L. Moore , and Lynn Morris Purpose of review To provide an update on neutralizing antibody targets in the context of the recent HIV-1 envelope trimer structure, describe new antibody isolation technologies, and discuss the implications of these data for HIV-1 prevention and therapy. Recent findings Recent advances in B-cell technologies have dramatically expanded the number of antibodies isolated from HIV-infected donors with broadly neutralizing plasma activity. These, together with the first high-resolution crystal and cryo-electron microscopy (cryo-EM) structures of a cleaved, prefusion HIV-1 trimer, have defined new regions susceptible to neutralization. This year, three epitopes in the gp120 – gp41 interface were structurally characterized, highlighting the importance of prefusion gp41 as a target. Similar to many other broadly neutralizing antibody epitopes, these new antibodies define a target that is also highly glycan dependent. Collectively, the epitopes for broadly neutralizing antibodies now reveal a continuum of vulnerability spanning the length of the HIV-1 envelope trimer. Summary Progress in the last year has provided support for the use of rationally stabilized whole HIV-1 trimers as immunogens for eliciting antibodies to multiple epitopes. Furthermore, the increasing number of broad and

Journal

Current Opinion in HIV and AidsWolters Kluwer Health

Published: May 1, 2015

There are no references for this article.