Novel HIV antibody identified
This study, led by Prof Florian Klein, Director of the Institute of Virology at the University Hospital of Cologne and Principle Investigator as well as Executive Board Member at the Center for Molecular Medicine Cologne (CMMC), opens up new perspectives for vaccine and therapeutic development against HIV-1 and was published in the journal Nature Immunology.
HIV-1 can be neutralized by antibodies when they bind to vulnerable structures on the virus surface. One such weak point is the so-called V3 glycan site of the virus's surface protein. This target structure plays a central role in the virus's entry into human cells and has therefore long been an important target for the development of new immunotherapeutic and preventive approaches. However, to date, it has mainly been possible to identify antibodies that can effectively recognize the V3 glycan site in only a fraction of the HIV variants circulating worldwide.
The antibody described here, designated 007, attacks the V3 glycan site in a different way than previously known antibodies. Unlike classic V3 antibodies, its binding does not depend on a specific sugar structure, which HIV-1 often modifies to evade the immune system. In laboratory tests, 007 therefore remains effective even against virus variants that are resistant to classic V3 antibodies. In a mouse model with human immune cells, 007 also effectively improves previous V3 antibody therapy, so that the virus must develop several changes simultaneously to evade antibody therapy. A key finding of the study is therefore that 007 closes previous gaps in the activity of classic V3 antibodies and thus supports antibody therapy combinations that can eliminate the virus more effectively overall.
“The V3 glycan site has long been considered a weak point of HIV-1, but until now it has only been possible to exploit it incompletely for therapeutic purposes and vaccine development,” explains lead author Dr Lutz Gieselmann from the Institute of Virology. Dr Malena Rohde, also an author of the paper and Co-Principle Investigator at the CMMC, adds: “The identification of antibody 007 shows that this weak spot is much more versatile than previously thought, opening up new perspectives for vaccine development.”
These research findings are therefore of great importance for the development of new combination therapies and vaccines. For use in HIV immunotherapy, 007 has already been exclusively licensed to Vir Biotechnology in collaboration with the Gates Foundation to promote its charitable purposes and is being developed preclinically with the support of the Cologne-based start-up company Togontech.
This study was supported by the Gates Foundation, the German Research Foundation (DFG), the German Center for Infection Research (DZIF), and the European Research Council (ERC).
Original Publication
https://www.nature.com/articles/s41590-025-02385-3
Lutz Gieselmann*, Andrew T. DeLaitsch*, Malena Rohde*, Caelan Radford, Johanna Worczinski, Anna Ashurov, Elvin Ahmadov, Judith A. Burger, Colin Havenar-Daughton, Sharvari Deshpande, Federico Giovannoni, Davide Corti, Christoph Kreer, Meryem Seda Ercanoglu, Philipp Schommers, Ivelin S. Georgiev, Anthony P. West Jr., Jacqueline Knüfer, Ricarda Stumpf, Arne Kroidl, Christof Geldmacher, Lucas Maganga, Wiston William, Nyanda E. Ntinginya, Michael Hoelscher, Zhengrong Yang, Qing Wei, Matthew B. Renfrow, Todd J. Green, Jan Novak, Marit J. van Gils, Harry B. Gristick, Henning Gruell, Jesse D. Bloom, Michael S. Seaman, Pamela J. Bjorkman & Florian Klein*, Identification of a potent V3 glycan site broadly neutralizing antibody targeting an N332gp120 glycan-independent epitope.Nat Immunol (2026). https://doi.org/10.1038/s41590-025-02385-3
Authors with CMMC affiliation indicated in bold and leading / first authors are indicated with a star (*) .
This message has been modified by the CMMC (K. Heber & D. Grosskopf-Kroiher) and is based on the text by the press and communications teams of the University Hospoital Cologne (original German version here).