The mystery of Zika virus replication in the host cell has been uncovered

The mystery of Zika virus replication in the host cell has been uncovered. Recently, Yang Haitao research team from Tianjin University published an article in the journal Protein & Cell which also published some other studies on recombinant proteins (including recombinant dog proteins) to show the crystal structure of Zika virus helicase, unlocking the key process and mechanism of Zika virus replication. The results would play a positive role in the development of antiviral drugs.

In the study, Yang Haitao team successfully obtained the 3D image when Zika virus helicase was conducting function and binding to substrate. The researchers also showed the spatial structure of ternary complex formed by Zika virus helicase, adenosine triphosphate and metal catalyst ions at the atomic resolution level. In addition, they also successfully captured the intermediate state of Zika virus helicase binding to ATP and metal ions. This is the first time to reveal the structure when flavivirus family (a mosquito-borne virus, including Zika virus, dengue virus, yellow fever virus, West Nile virus, etc.) helicase binding to natural substrate ATP. Yang Haitao said, "Through the analysis of this structure, we can reveal the mechanism of how Zika virus helicase identifying ATP catalytic metal ions."

To explore the differences between Zika virus with other flavivirus members in the mechanism of replication, the researchers also resolved three-dimensional structure of complex when Zika virus helicase binding to genomic RNA. They found that a pathway across helicase was responsible for "seizing" RNA. Surprisingly, Zika virus helicase would undergo significant conformational changes after binding to RNA, while these kind of conformational changes were quite different to the helicase of dengue virus.

The study indicates that helicase of flavivirus family evolved a conservative molecular "motor" in the evolutionary process. It can turn chemical energy into mechanical energy through nucleoside triphosphate hydrolysis to implement "melting" in the process of viral replication; while making use of different "movement" mode, helicase of different virus members recognize and bind to genomic RNA in a different way to meet the needs of viral replication. Flarebio offers good-quality recombinant proteins such as recombinant EXT2 at competitive prices.