Wednesday, September 14, 2016

Scientists reveal the structure of the protein NS1 Zika

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Scientists reveal the structure of the protein NS1 Zika -

Researchers have revealed the molecular structure of a protein produced by Zika virus which is thought to be involved in reproduction of the virus and its interaction with the host immune system.

results provide scientists around the world with new information on the role of NS1 protein in the Zika virus infections, and expands the scientists' understanding of the flavivirus family, which also includes dengue , West Nile and yellow fever.

The study was conducted by the University of Michigan and in collaboration with Purdue University.

"Having the structure of the full-length NS1 Zika provides new information that can help guide the design of a potential vaccine or antiviral drugs," said lead author Janet Smith, director of the Center for structural biology at the UM Institute for life sciences, where his laboratory is located and biological chemistry professor at the UM Medical School.

"Researchers are still working to understand precisely how Zika and other flavivirus interact with the immune system of an infected person," she said. "Having these details at the atomic level can help scientists ask better questions and to design more thoughtful experiences that we continue to learn new information. "

The results are scheduled for publication online July 25 in Nature Structural & Molecular Biology. Earlier this year, scientists in China have published a partial structure.

The virus transmitted by mosquitoes Zika has been around for decades, but recently grew up in a situation of international health emergency as a result of its association with severe birth defects and Guillain-Barre syndrome and its rapid spread in Central and South America.

There are currently no treatment or vaccine, though several companies have announced plans to try to develop.

"Despite its similarity to other related viruses, we found that the structure Zika NS1 were some important differences," said W. Clay Brown, scientific director of the Centre top speed laboratory biology protein structural and co-first author of the study.

the new 3-D structure, which was obtained by crystal X-ray and electron microscopy revealed that the outer surface of the protein NS1 Zika significantly the different electrical properties, load than other flavivirus saying it may interact differently with members of the immune system of an infected person.

This study was also the first to capture the molecular structure of loops flexible on areas of the wing of the protein, which had been hidden from view in previous studies.

"of NS1 structural studies in dengue this loop was thought flipped up, but our study shows that Zika virus flips down the wings, "said co-author Richard Kuhn, professor of biological sciences at Purdue University and director of the Purdue Institute of inflammation, immunology and infectious diseases. "This is very important because it indicates an interaction with the cell membrane of the host and a possible mechanism by which NS1 exerts its multiple functions.

" Seeing this difference provides new perspectives that help us understand the NS1 protein, "said Kuhn, who was a member of the research team that first determines the structure of the Zika virus." understanding the structure and function help us identify targets for inhibitors block major viral processes and treat the infection. "

the team also examined changes in the genetic sequence of the protein NS1 Zika over time, noted David L. Akey, researcher in the laboratory Smith and other senior author of the study.

"Like the common cold and flu viruses change over time, the Zika virus has changed over its spread around the world so that NS1 in Brazilian infections seems different to the immune system his African ancestor, "said Akey.

NS1 (nonstructural protein 1) protein plays several roles in viral infections. Inside the infected cells, it is essential to make new copies of the virus to infect additional cells. Infected cells also secrete NS1 packets in the patient's bloodstream, where higher levels were associated with more severe disease.

The protein cross-shaped with two distinct surfaces. The inner surface is "fat" and is believed to interact with cell membranes, while the outer surface, once secreted into the blood, can interact with the patient's immune system.

Even in the absence of this virus, the secreted version of some NS1 proteins can create vascular bleeding, as seen in cases of severe dengue.

in 2014, many of the same members of the team participated in the first study to isolate and map the NS1 protein of dengue and West Nile virus, which appeared in the journal Science . "Isolate Protein to study it has been a challenge for researchers," said Smith at the time. "Once we found out how to do this, it crystallizes beautifully."


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