A team led by scientists at the National Institutes of Health (NIH) has reported a research trifecta. They discovered a new vulnerable site on HIV for a vaccine to target, a broadly neutralizing antibody that binds to that target site, and how the antibody stops the virus from infecting a cell. The study was led by scientists at the Vaccine Research Center (VRC) of the National Institute of Allergy and Infectious Diseases, part of NIH.
This is a model of the VRC34.01 antibody (green and yellow) bound to the fusion peptide (red) on a spike on HIV's surface (gray). Courtesy of NIAID
A team led by scientists at the National Institutes of Health (NIH) has reported a research trifecta. They discovered a new vulnerable site on HIV for a vaccine to target, a broadly neutralizing antibody that binds to that target site, and how the antibody stops the virus from infecting a cell. The study was led by scientists at the Vaccine Research Center (VRC) of the National Institute of Allergy and Infectious Diseases, part of NIH.
The new target is a part of HIV called the fusion peptide, a string of eight amino acids that helps the virus fuse with a cell to infect it. The fusion peptide has a much simpler structure than other sites on the virus that HIV vaccine scientists have studied.
The scientists first examined the blood of an HIV-infected person to explore its ability to stop the virus from infecting cells. The blood was good at neutralizing HIV but did not target any of the vulnerable spots on the virus where broadly neutralizing HIV antibodies (bnAbs) were known to bind.
The researchers isolated a powerful bnAb in the blood that they named VRC34.01, and found that it binds to the fusion peptide and a sugar molecule. The scientists then crystallized the antibody while it was bound to the virus. This allowed them to characterize in atomic-level detail how VRC34.01 attaches to HIV and revealed that the antibody stops the virus from infecting a cell by binding to a key cell-surface molecule.
The scientists also report that it is not unusual for the immune system to try to stop HIV from infecting a cell by attacking the fusion peptide. When they screened the blood of 24 HIV-infected volunteers, they found that blood samples from 10 people targeted a similar binding site as VRC34.01.
The researchers are now working to create a vaccine designed to elicit antibodies similar to the VRC34.01 antibody.
Reference: Kong R, et al. Fusion peptide of HIV-1 as a site of vulnerability to neutralizing antibody. Science DOI: 10.1126/science.aae0474 (2016).
Source: NIH/National Institute of Allergy and Infectious Diseases
A Helping Hand: Innovative Approaches to Expanding Hand Hygiene Programs in Acute Care Settings
July 9th 2025Who knew candy, UV lights, and a college kid in scrubs could double hand hygiene adherence? A Pennsylvania hospital’s creative shake-up of its infection prevention program shows that sometimes it takes more than soap to get hands clean—and keep them that way.
Broadening the Path: Diverse Educational Routes Into Infection Prevention Careers
July 4th 2025Once dominated by nurses, infection prevention now welcomes professionals from public health, lab science, and respiratory therapy—each bringing unique expertise that strengthens patient safety and IPC programs.
How Contaminated Is Your Stretcher? The Hidden Risks on Hospital Wheels
July 3rd 2025Despite routine disinfection, hospital surfaces, such as stretchers, remain reservoirs for harmful microbes, according to several recent studies. From high-touch areas to damaged mattresses and the effectiveness of antimicrobial coatings, researchers continue to uncover persistent risks in environmental hygiene, highlighting the critical need for innovative, continuous disinfection strategies in health care settings.