By cashing-in on the interaction between a virus and antibodies that fight infection, Princeton University scientists may have discovered a better way to make a vaccine against the flu virus.
The researchers have said that by manipulating the multi-stage interactive process- called antibody interference-to advantage, it could be possible to design more powerful vaccines than exist today.
"We have proposed that antibody interference plays a major role in determining the effectiveness of the antibody response to a viral infection. And we believe that in order to get a more powerful vaccine, people are going to want one that minimizes this interference," said Ned Wingreen, a professor of molecular biology.
When Ndifon and colleagues analysed data about viral structure, antibody types and the reactions between them produced by virology laboratories across the country, they noticed a confusing pattern.
They found that antibodies were often better at protecting against a slightly different virus, a close cousin, than against the virus that spurred their creation-a process known as cross-reactivity.
On a closer look, they found that a phenomenon known as antibody interference was at play-it arises when a virus prompts the creation of multiple types of antibodies.
As a result, during a viral attack, antibodies vie with each other to defend the body, and sometimes crowd each other out while they attempt to attach themselves to the surface of the virus.
But, strangely, antibodies that are actually less effective at protecting the body against a specific virus are also equally adept at attaching themselves to the virus, blocking the more effective antibodies from doing their job.
Thus, the scientists have suggested that if a way can be found to weaken the binding of the less effective antibodies, this might constitute a new approach to vaccine design.
The researchers claimed that the pattern of enhanced cross-reactivities could easily be attributed to viruses that differ only at the sites on their surfaces where the less effective antibodies bind.
Such variants would make ideal vaccine strains, guiding the immune system to produce two distinct types of antibodies: effective ones that are well matched to and good at binding to the infecting virus, and ineffective ones that are poorly matched to and bad at binding to the infecting virus, and consequently stay out of the way.
The findings have been described in the online edition of the Proceedings of the National Academy of Sciences.