A team of researchers from Purdue University led by Richard Kuhn, director of the Purdue Institute for Inflammation, Immunology and Infectious Diseases (PI4D), with Michael Rossmann, Purdue's Hanley Distinguished Professor of Biological Sciences has determined the structure of the Zika virus, which reveals insights critical to the development of effective antiviral treatments and vaccines. The research team identified regions within the Zika virus structure where it differs from other flaviviruses.

They found that all of the known flavivirus structures differ in the amino acids that surround a glycosylation site in the virus shell. The shell is made up of 180 copies of two different proteins. The glycosylation site where Zika virus differs from other flaviviruses protrudes from the surface of the virus. In many other viruses, it has been shown that as the virus projects a glycosylation site outward, an attachment receptor molecule on the surface of a human cell recognizes the sugars and binds to them. The virus is like a menacing stranger luring an unsuspecting victim with the offer of sweet candy. The human cell gladly reaches out for the treat and then is caught by the virus, which, once attached, may initiate infection of that cell.

The team studied a Zika virus strain isolated from a patient infected during the French Polynesia epidemic and determined the structure to 3.8Å. At this near-atomic resolution, key features of the virus structure can be seen and groups of atoms that form specific chemical entities, such as those that represent one of 20 naturally occurring amino acids, can be recognized, according to Rossmann.

For more details, read the news release at Purdue University website.