A team of researchers recently mapped the co-crystalline tool that a human antibody can use to neutralize the influenza viruses.
Scientists from the Scripps Research Institute and Sea Lane Biotechnologies found that the antibody can recognize the structure flu viruses use to attach themselves to host cells. The structure was previously believed to be too small for an antibody to latch onto effectively, according to ScienceDaily.com.
The antibody is capable of using a small portion of its target-grappling apparatus to hit this precise point on multiple strains of the flu virus.
“This highly focused binding to the receptor binding site using only a single loop on the antibody has never been seen before, and it’s really fascinating; it gives us some good ideas about designs for vaccines and therapies,” Ian A. Wilson, a senior investigator from Scripps research, said, ScienceDaily.com reports.
The team began by collecting bone marrow samples from patients known to have been exposed to certain key influenza strains. Bone marrow contains a record of all of the antibodies produced by the body. Sea Lane then used the data to create a comprehensive library of billions of antibody records.
The scientists screened the enormous library and eventually isolated an unusual antibody, dubbed C05, that can bind to influenza A viruses. The antibody proved capable of defending cells from infection and also worked as a therapy if administered up to three days after infection.
“If we can figure out how to induce this sort of antibody in a vaccine, we would have something that’s very useful,” Lawrence Horowitz, the CEO of Sea Lane Biotechnologies, said, ScienceDaily.com reports.