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HIV vaccine: the human immune system recognizes key sites of HIV infection and attacks the virus
Last reviewed: 01.07.2025
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HIV is covered in a glycoprotein shell that hides the virus from attack by the immune system. A newly published study shows how neutralizing antibodies to HIV use part of the glycoprotein shell to bind to the virus. The binding site of the antibodies is called the V1/V2 region, and scientists say it is a good target for an HIV vaccine.
In addition, their study reveals the detailed structure of the V1/V2 region at the atomic level.
The study was led by Peter D. Kwon, chief of the Vaccine Research Center at the National Institute of Allergy and Infectious Diseases (NIAID).
Some people who have been infected with HIV begin to produce antibodies over several years that can neutralize a wide range of strains of the virus. These neutralizing antibodies bind to one of four sites on the virus that includes a glycoprotein called amino acid residue 160. The glycoproteins are arranged in the spikes of HIV.
New research shows how the HIV neutralizing antibody PG9 disarms the virus by latching onto a glycoprotein at residue 160, along with part of a second glycoprotein, a short amino acid residue sequence in the V1/V2 region of the HIV spike.
Similarly, a separate, recently published study from the Scripps Research Institute showed how different HIV neutralizing antibodies bind to the virus via two glycoproteins and a sequence of amino acid residues. Taken together, the two studies suggest that in some cases, the combination of a viral glycoprotein and an amino acid can form the binding site of HIV neutralizing antibodies.
Recent blood tests have shown that study participants who were vaccinated and then developed antibodies to the V1/V2 region were less likely to become infected. Although the role of these antibodies in protecting against HIV is unknown, this finding highlights the importance of understanding V1/V2 antibodies in developing a more effective HIV vaccine.