Protein Critical to Zika Virus Found
Credit: Cheng Kao, Indiana University
Zika virus is a mosquito-borne infectious disease linked to certain birth defects in infants in South and Central America and the United States. A Lawrence Berkeley National Laboratory (Berkeley Lab) researcher, Banumathi Sankaran, worked as part of a multi-institutional team to map a key viral protein called NS5. Necessary to virus reproduction, NS5 contains two enzyme activities: one reduces the body’s ability to mount an immune response against infection and the other helps start the genetic replication process. The work was led by Indiana University’s Cheng Kao and Pingwei Li at Texas A&M University (TAMU).
In a study published March 27 in Nature Communications, the team described the structure and function of these two enzyme active sites. They also showed comparisons between this protein and those from other related viruses that cause dengue fever, West Nile virus, Japanese encephalitis virus, and hepatitis C. These comparisons will help researchers as they search for possible compounds to halt the ability of the virus to reproduce.
Working with researchers from TAMU, Sankaran, a research scientist in the Molecular Biophysics and Integrated Bioimaging Division at Berkeley Lab, used X-ray crystallography to solve the atomic structure of NS5 in the Berkeley Center for Structural Biology at the Advanced Light Source (ALS). “The ALS was critical to the success of this project,” said Li. “The powerful beam and the sensitive detector on beamline 5.0.2 made it possible for us to obtain data on our poor quality crystals.”
Sankaran is in charge of the Collaborative Crystallography (CC) program at the ALS. Funded by the NIH, this program is a fast, reliable and transparent mail-in crystallographic service for the structural biology community. Since the mosquitos carrying the vector have been spreading into the Southern U.S., interest in studying the virus has increased and TAMU’s Li indicated that several groups currently are working on similar structural determination efforts. “Having access to state-of-the-art facilities provided by our Collaborative Crystallography program resulted in a rapid turnaround of this project,” according to Sankaran.
While the researchers have gathered a lot of information about how to target this protein, there are still puzzles remaining. “One of the most important unresolved questions about Zika NS5 is how it catalyzes the synthesis of RNA,” said Li. “We look forward to further studies and future collaborations, which will be invaluable for therapeutics discovery.”
Zhao, B., Yi, G., Du, F., Chuang, Y., Vaughan, R. C., Sankaran, B., . . . Li, P. (2017). Structure and function of the Zika virus full-length NS5 protein. Nature Communications, 8, 14762. doi:10.1038/ncomms14762
This article has been republished from materials provided by Berkeley Lab. Note: material may have been edited for length and content. For further information, please contact the cited source.
Cell Recycling System Offers Therapeutic Entry Point for Rare Disease TreatmentNews
Scientists have demonstrated how an investigational drug works against a rare, fatal genetic disease, Niemann-Pick type C1 (NPC1).READ MORE
Material From Shellfish Boosts Sensitivity of Diagnostic TestsNews
By adding polydopamine at a key step, the sensitivity of diagnostic tests and bioassays can be increased by as many as 100 to 1,000 times.READ MORE
Microscopy Technique Could Enable More Informative BiopsiesNews
MIT and Harvard Medical School researchers have devised a way to image biopsy samples with much higher resolution — an advance that could help doctors develop more accurate and inexpensive diagnostic tests.READ MORE
Comments | 0 ADD COMMENT
EMBL Conference: European Conference of Life Science Funders and Foundations
Apr 19 - Apr 20, 2018
EMBO Workshop: Integrating Systems Biology: From Networks to Mechanisms to Models
Apr 15 - Apr 17, 2018
EMBL Course: Introduction to Metabolomics Analysis
Mar 20 - Mar 23, 2018