A broad antibody with enhanced HIV-1 neutralization via bispecific antibody-mediated prepositioning

Abstract Antibodies targeting the highly conserved prehairpin intermediate (PHI) of class I viral membrane-fusion proteins are generally weakly neutralizing and are not considered viable therapeutic agents. We previously demonstrated that antibodies targeting the gp41 N-heptad repeat (NHR), which is...

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Main Authors: Soohyun Kim, Caelan E. Radford, Duo Xu, Jianing Zhong, Jonathan Do, Dominic M. Pham, Katie A. Travisano, Maria V. Filsinger Interrante, Theodora U. J. Bruun, Valerie Rezek, Bailey Wilder, Martina Palomares, Michael S. Seaman, Scott G. Kitchen, Jesse D. Bloom, Peter S. Kim
Format: Article
Language:English
Published: Nature Portfolio 2025-05-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-025-60035-6
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author Soohyun Kim
Caelan E. Radford
Duo Xu
Jianing Zhong
Jonathan Do
Dominic M. Pham
Katie A. Travisano
Maria V. Filsinger Interrante
Theodora U. J. Bruun
Valerie Rezek
Bailey Wilder
Martina Palomares
Michael S. Seaman
Scott G. Kitchen
Jesse D. Bloom
Peter S. Kim
author_facet Soohyun Kim
Caelan E. Radford
Duo Xu
Jianing Zhong
Jonathan Do
Dominic M. Pham
Katie A. Travisano
Maria V. Filsinger Interrante
Theodora U. J. Bruun
Valerie Rezek
Bailey Wilder
Martina Palomares
Michael S. Seaman
Scott G. Kitchen
Jesse D. Bloom
Peter S. Kim
author_sort Soohyun Kim
collection DOAJ
description Abstract Antibodies targeting the highly conserved prehairpin intermediate (PHI) of class I viral membrane-fusion proteins are generally weakly neutralizing and are not considered viable therapeutic agents. We previously demonstrated that antibodies targeting the gp41 N-heptad repeat (NHR), which is transiently exposed in the HIV-1 PHI, exhibit enhanced broad neutralization in cells expressing the Fc receptor, FcγRI. To enhance neutralization in cells lacking FcγRI, we here develop a bispecific antibody (bsAb) by fusing an NHR-targeting antibody to an antibody against CD4, the HIV-1 receptor on T cells. The bsAb provides a 5000-fold neutralization enhancement and shows unprecedented neutralization breadth compared to existing broadly neutralizing antibodies. Importantly, the bsAb reduces viral load in HIV-1-infected humanized male mice, and viral envelope sequencing under bsAb pressure revealed an NHR mutation that potentially impairs viral fitness. These findings validate the NHR as a potential HIV-1 therapeutic target, setting the stage for a new class of broadly neutralizing antibodies.
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spelling doaj-art-42690c827ba64d56b04488cfc6be4c1b2025-08-20T02:25:13ZengNature PortfolioNature Communications2041-17232025-05-0116111410.1038/s41467-025-60035-6A broad antibody with enhanced HIV-1 neutralization via bispecific antibody-mediated prepositioningSoohyun Kim0Caelan E. Radford1Duo Xu2Jianing Zhong3Jonathan Do4Dominic M. Pham5Katie A. Travisano6Maria V. Filsinger Interrante7Theodora U. J. Bruun8Valerie Rezek9Bailey Wilder10Martina Palomares11Michael S. Seaman12Scott G. Kitchen13Jesse D. Bloom14Peter S. Kim15Department of Biochemistry, Stanford University School of MedicineMolecular and Cellular Biology Graduate Program, University of Washington and Basic Sciences Division, Fred Hutchinson Cancer CenterDepartment of Biochemistry, Stanford University School of MedicineDepartment of Chemistry, Stanford UniversityDepartment of Biochemistry, Stanford University School of MedicineSarafan ChEM-H, Stanford UniversityDepartment of Microbiology & Immunology, Stanford University School of MedicineSarafan ChEM-H, Stanford UniversityDepartment of Biochemistry, Stanford University School of MedicineDepartment of Medicine, Division of Hematology and Oncology, David Geffen School of Medicine at University of California, Los Angeles (UCLA)Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical SchoolCenter for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical SchoolCenter for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical SchoolDepartment of Medicine, Division of Hematology and Oncology, David Geffen School of Medicine at University of California, Los Angeles (UCLA)Basic Sciences Division and Computational Biology Program, Fred Hutchinson Cancer CenterDepartment of Biochemistry, Stanford University School of MedicineAbstract Antibodies targeting the highly conserved prehairpin intermediate (PHI) of class I viral membrane-fusion proteins are generally weakly neutralizing and are not considered viable therapeutic agents. We previously demonstrated that antibodies targeting the gp41 N-heptad repeat (NHR), which is transiently exposed in the HIV-1 PHI, exhibit enhanced broad neutralization in cells expressing the Fc receptor, FcγRI. To enhance neutralization in cells lacking FcγRI, we here develop a bispecific antibody (bsAb) by fusing an NHR-targeting antibody to an antibody against CD4, the HIV-1 receptor on T cells. The bsAb provides a 5000-fold neutralization enhancement and shows unprecedented neutralization breadth compared to existing broadly neutralizing antibodies. Importantly, the bsAb reduces viral load in HIV-1-infected humanized male mice, and viral envelope sequencing under bsAb pressure revealed an NHR mutation that potentially impairs viral fitness. These findings validate the NHR as a potential HIV-1 therapeutic target, setting the stage for a new class of broadly neutralizing antibodies.https://doi.org/10.1038/s41467-025-60035-6
spellingShingle Soohyun Kim
Caelan E. Radford
Duo Xu
Jianing Zhong
Jonathan Do
Dominic M. Pham
Katie A. Travisano
Maria V. Filsinger Interrante
Theodora U. J. Bruun
Valerie Rezek
Bailey Wilder
Martina Palomares
Michael S. Seaman
Scott G. Kitchen
Jesse D. Bloom
Peter S. Kim
A broad antibody with enhanced HIV-1 neutralization via bispecific antibody-mediated prepositioning
Nature Communications
title A broad antibody with enhanced HIV-1 neutralization via bispecific antibody-mediated prepositioning
title_full A broad antibody with enhanced HIV-1 neutralization via bispecific antibody-mediated prepositioning
title_fullStr A broad antibody with enhanced HIV-1 neutralization via bispecific antibody-mediated prepositioning
title_full_unstemmed A broad antibody with enhanced HIV-1 neutralization via bispecific antibody-mediated prepositioning
title_short A broad antibody with enhanced HIV-1 neutralization via bispecific antibody-mediated prepositioning
title_sort broad antibody with enhanced hiv 1 neutralization via bispecific antibody mediated prepositioning
url https://doi.org/10.1038/s41467-025-60035-6
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