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Fragment of yellow fever virus may hold key to safer vaccine

dress on the envelope protein. Several other amino acids in another section of the folded protein contributed to the neutralization.

Yellow fever virus--and its flavivirus cousins, including dengue and West Nile –look like balls covered by approximately 100 cross-hatched pairs of envelope proteins lying on the surface. The prongs of Y-shaped antibodies against yellow fever likely span the pairs by grabbing the essential epitope on one and the supporting amino acids on the other, ter Meulen speculates. The findings may apply to the whole flavivirus family.

The results confirm and extend similar studies in mice, but the human antibody-virus binding configuration looks more complex, ter Meulen said.

In theory, the crucial antibodies, which have been cloned, could be used for prophylactic protection after suspected exposure, or for therapy, but ter Meulen does not think that pharmaceutical companies are likely to take this approach. More realistically, he said, the findings could help manufacturers design a more consistent vaccine based on recombinant genetic technology, without the potential side effects from variations of the weakened virus strain now grown in fertilized chicken eggs.


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Source:Howard Hughes Medical Institute


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