The monomeric structure of ZIKV helicase. (A) Size-exclusion chromatograms of ZIKV helicase. The molecular masses of protein standards are indicated at the top. (B) The overall structure of ZIKV helicase with the three domains colored and labeled respectively. (C) A cartoon diagram illustrating of the overall fold with potential RNA binding site and NTPase active site labelled. (D) Structure-based phylogenetic tree of 8 viral helicase structures from the Flaviviradae family using the program SHP (Stuart et al., 1979) and PHYLIP (Felsenstein, 1997). The following structures with PDB ID in parentheses are included: DENV-2 (2BMF), DENV-4 (2JLQ), JEV (2Z83), KUNV (2QEQ), YFV (1YKS), MVEV (2V8O), HCV (1HEI)
A team led by researchers from Tianjin University (P.R. China) has solved the structure of Zika virus helicase. Zika virus can cause microcephaly and other severe birth defects. However, as there are currently no effective vaccines or therapies available to contain ZIKV infection, ZIKV remains a significant challenge to public health.
All viruses seem to need a helicase for replication. The Zika virus helicase is a motor enzyme which can convert energy from nucleoside triphosphate to unwind double stranded nucleic acids. This is an essential step for viral replication. By targeting Zika virus helicase with small-molecule inhibitors, it might be possible to stop viral replication and prevent disease. The scientists have successfully obtained an image at 1.8 angstroms of this viral enzyme. An angstrom is one ten-billionth of a meter. This high-resolution image of the Zika virus key enzyme will help scientists develop drugs to treat the Zika virus disease. http://www.eurekalert.org/pub_releases/2016-05/s-rst052016.php
http://link.springer.com/article/10.1007%2Fs13238-016-0275-4
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