MedicalResearch.com Interview with:
Dr. Jikui Song PhD
Assistant professor of biochemistry
University of California, Riverside.
MedicalResearch.com: What is the background for this study? What are the main findings?
Response: Recent outbreak of Zika virus (ZIKV) has become a wordwide health concern. However, no vaccines or antiviral drugs against ZIKV are currently available. To explore potential druggable sites for ZIKV, we set out to determine the crystal structure of full-length ZIKV NS5, the molecular machinery responsible for the genomic replication of ZIKV.
The major findings of our study include the identification of a conserved domain conformation within flavivirus NS5 family, which may be important for functional regulation of flavivirus NS5. Furthermore, our structural analysis revealed a potential drug-binding site of ZIKV NS5, providing basis for future development of novel antivirals against ZIKV.
MedicalResearch.com: What should readers take away from your report?
Response: The structural homology between ZIKV NS5 and other flavivirus NS5 proteins makes it possible to develop the inhibitors for ZIKV NS5 based on the inhibitors that have been identified for other flavivirus NS5 proteins, such as dengue virus NS5.
MedicalResearch.com: What recommendations do you have for future research as a result of this study?
Response: It’s possible to explore structure-based drug design targeting ZIKV NS5 based on the protein structure determined in this study.
MedicalResearch.com: Thank you for your contribution to the MedicalResearch.com community.
The structure of Zika virus NS5 reveals a conserved domain conformation
Boxiao Wang, Xiao-Feng Tan, Stephanie Thurmond, Zhi-Min Zhang, Asher Lin, Rong Hai & Jikui Song
Nature Communications 8, Article number: 14763 (2017)
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