Anti-V2 antibodies virus vulnerability revealed by envelope V1 deletion in HIV vaccine candidates
Isabela Silva de Castro, Giacomo Gorini, Rosemarie D. Mason, Jason Gorman, Massimiliano Bissa, Mohammad Arif Rahman, Anush Arakelyan, Irene Kalisz, Stephen Whitney, Manuel Becerra‐Flores, Eric Ni, Kristina K. Peachman, Hung V. Trinh, Michael J. Read, Mei-Hue Liu, Donald Van Ryk, Dominic Paquin‐Proulx, Zhanna Shubin, Marina Tuyishime, Jennifer Peele, Mohammed S. Ahmadi, Raffaello Verardi, Juliane P. Hill, Margaret H. Beddall, Richard Nguyen, James D. Stamos, Dai Fujikawa, Susie Min, Luca Schifanella, Monica Vaccari, Veronica Galli, Melvin N. Doster, Namal P. M. Liyanage, Sarkis Sarkis, Francesca Caccuri, Celia C. LaBranche, David C. Montefiori, Georgia D. Tomaras, Xiaoying Shen, Margherita Rosati, Barbara K. Felber, George N. Pavlakis, David Venzon, William Magnanelli, Matthew W. Breed, Josh Kramer, Brandon F. Keele, Michael A. Eller, Claudia Cicala, James Arthos, Guido Ferrari, Leonid Margolis, Marjorie Robert-Guroff, Peter D. Kwong, Mario Roederer, Mangala Rao, Timothy Cardozo, Genoveffa Franchini
Abstract
integrin. SIV vaccines engineered to delete V1 and favor an α helix, rather than a β sheet V2 conformation, induced V2-specific ADCC correlating with decreased risk of SIV acquisition. Removal of V1 from the HIV-1 clade A/E A244 envelope resulted in decreased binding to antibodies recognizing V2 in the β sheet conformation. Thus, deletion of V1 in HIV envelope immunogens may improve antibody responses to V2 virus vulnerability sites and increase the efficacy of HIV vaccine candidates.