Scientists Resolve Crystal Structure of Zika Virus Replicase at 1.8-Angstroms; Possible Basis for Anti-Viral Drug Design

A team led by researchers from Tianjin University (People’s Republic of China) has solved the structure of the Zika virus helicase, which is a key target for antiviral development. The research is published online in May 12, 2016 in Springer's journal Protein & Cell. The open-access article is titled “The Crystal Structure of Zika Virus Helicase: Basis for Antiviral Drug Design.” The Zika virus (ZIKV) 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 ZIKV helicase is a motor enzyme that can convert energy from nucleoside triphosphate to unwind-double stranded nucleic acids. This is an essential step for viral replication. By targeting ZIKV 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 the ZIKV helicase. This high-resolution image of the ZIKV key enzyme may help scientists develop drugs to treat the ZIKV disease. The image here is from the article in Protein & Cell and is also reproduced in the press release. (Credit: Protein & Cell). Please see either the article or the press release to view a larger version of this image. [Press release] [Protein & Cell article]
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