According to a report in the journal Science, an experimental vaccine to protect against respiratory syncytial virus (RSV) elicited high levels of RSV-specific antibodies when tested in animals.

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Scientists from the Vaccine Research Center (VRC), National Institute of Allergy and Infectious Diseases (NIAID), part of the National Institutes of Health (NIH), expanded on previous findings about the structure of a critical viral protein to design the vaccine.

In a natural RSV infection, the immune system produces antibodies against both the pre-fusion and post-fusion forms of F glycoprotein, a type of RSV protein. But the antibodies to antigenic site zero, which is only present on the pre-fusion form, have much stronger neutralizing activity. 

Researchers deduced that a vaccine against RSV would have a higher chance of success by eliciting antibodies directed at F glycoprotein in its pre-fusion configuration.

In animal tests, the researchers found that the more stable the protein, the higher the levels of neutralizing antibodies elicited by vaccination. The levels of antibody made in response to one of the engineered F glycoproteins were more than 10 times higher than those produced following vaccination with post-fusion F glycoprotein and well above levels needed to protect against RSV infection.

Scientists hope to launch early-stage human clinical trials of this candidate RSV vaccine as soon as clinical grade material can be manufactured.

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