Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

Cracking a virus protection shield

16.06.2006
Ebola, measles and rabies are serious threats to public health in developing countries. Despite different symptoms all of the diseases are caused by the same class of viruses that unlike most other living beings carry their genetic information on a single RNA molecule instead of a double strand of DNA.

Now researchers from the Institut de Virologie Moléculaire et Structurale (IVMS) and the Outstation of the European Molecular Biology Laboratory (EMBL) in Grenoble have obtained a detailed structural picture of a protein that allows the rabies virus to withstand the human immune response and survive and replicate in our cells. The study that is published in this week’s online edition of Science suggests new potential drug targets in rabies and sheds light on how similar approaches can help fighting other viral diseases.

When the rabies virus enters a human cell through the membrane, the RNA molecule that carries its genes is transported into the centre of the cell. Here it redirects the cellular machinery of the host to produce many new copies of the virus that go on to infect more cells. One molecule that is crucial in this process is a viral protein called nucleoprotein. The protein ensures that on its way through the cell the virus RNA is not destroyed by the immune response of the host.

“Nucleoprotein is vital for the rabies virus,” says Rob Ruigrok, Head of the IVMS. “It is one of the few proteins that the virus brings into the host cell and it wraps around the RNA like a protection shield. Without this shield the RNA would be degraded by the enzymes of the human immune system that try to eliminate the invader.”

To investigate how exactly this protection shield works, Aurélie Albertini from Ruigrok’s team obtained crystals of nucleoprotein bound to RNA. Examining the crystals with high-intensity X-ray sources at the European Synchrotron Radiation Facility (ESRF), Amy Wernimont from Winfried Weissenhorn’s group at EMBL Grenoble produced a high-resolution image of the protein.

“Nucleoprotein acts like a clamp,” says Weissenhorn. “It consists of two domains that like two jaws clasp around the RNA strand. Many nucleoproteins bind side-by-side along the length of an RNA molecule and make it inaccessible for degrading enzymes but also for the machinery needed to replicate the virus. This means that the protection shield must be flexible and able to distinguish between different types of enzymes trying to gain access.”

The detailed structural picture suggests that upon a signal a part of the protein located between the two main domains might act as a hinge that moves the upper jaw out of the way when time for replication has come.

“This dynamic mechanism makes nucleoproteins an excellent drug target,” says Ruigrok, “Small agents that bind to the protein in such a way to block its flexibility and keep it in the closed state, would prevent replication of the virus and would stop it from spreading.”

Rabies virus shares this protection strategy with other viruses of its class; in Ebola, measles and Borna virus similar complexes of RNA and nucleoproteins have been found.

“This means that our results do not only have implications for the design of new drugs against rabies, but they suggest new therapeutic approaches in a variety of diseases, some of which are much more threatening than rabies. On a different note, the conservation of the nucleoprotein system also leaves room for evolutionary speculations about common ancestors and primordial infectious units of RNA viruses,” Weissenhorn concludes.

Anna-Lynn Wegener | alfa
Further information:
http://www.embl.org/aboutus/news/press/2006/16jun06/index.html

More articles from Life Sciences:

nachricht Key discoveries offer significant hope of reversing antibiotic resistance
23.10.2017 | University of Bristol

nachricht Introduction of a novel system for in vitro analyses of zebrafish oligodendrocyte progenitor cells
23.10.2017 | DFG-Forschungszentrum für Regenerative Therapien TU Dresden

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

Die letzten 5 Focus-News des innovations-reports im Überblick:

Im Focus: Neutron star merger directly observed for the first time

University of Maryland researchers contribute to historic detection of gravitational waves and light created by event

On August 17, 2017, at 12:41:04 UTC, scientists made the first direct observation of a merger between two neutron stars--the dense, collapsed cores that remain...

Im Focus: Breaking: the first light from two neutron stars merging

Seven new papers describe the first-ever detection of light from a gravitational wave source. The event, caused by two neutron stars colliding and merging together, was dubbed GW170817 because it sent ripples through space-time that reached Earth on 2017 August 17. Around the world, hundreds of excited astronomers mobilized quickly and were able to observe the event using numerous telescopes, providing a wealth of new data.

Previous detections of gravitational waves have all involved the merger of two black holes, a feat that won the 2017 Nobel Prize in Physics earlier this month....

Im Focus: Smart sensors for efficient processes

Material defects in end products can quickly result in failures in many areas of industry, and have a massive impact on the safe use of their products. This is why, in the field of quality assurance, intelligent, nondestructive sensor systems play a key role. They allow testing components and parts in a rapid and cost-efficient manner without destroying the actual product or changing its surface. Experts from the Fraunhofer IZFP in Saarbrücken will be presenting two exhibits at the Blechexpo in Stuttgart from 7–10 November 2017 that allow fast, reliable, and automated characterization of materials and detection of defects (Hall 5, Booth 5306).

When quality testing uses time-consuming destructive test methods, it can result in enormous costs due to damaging or destroying the products. And given that...

Im Focus: Cold molecules on collision course

Using a new cooling technique MPQ scientists succeed at observing collisions in a dense beam of cold and slow dipolar molecules.

How do chemical reactions proceed at extremely low temperatures? The answer requires the investigation of molecular samples that are cold, dense, and slow at...

Im Focus: Shrinking the proton again!

Scientists from the Max Planck Institute of Quantum Optics, using high precision laser spectroscopy of atomic hydrogen, confirm the surprisingly small value of the proton radius determined from muonic hydrogen.

It was one of the breakthroughs of the year 2010: Laser spectroscopy of muonic hydrogen resulted in a value for the proton charge radius that was significantly...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

Event News

3rd Symposium on Driving Simulation

23.10.2017 | Event News

ASEAN Member States discuss the future role of renewable energy

17.10.2017 | Event News

World Health Summit 2017: International experts set the course for the future of Global Health

10.10.2017 | Event News

 
Latest News

Introduction of a novel system for in vitro analyses of zebrafish oligodendrocyte progenitor cells

23.10.2017 | Life Sciences

Did you know how many parts of your car require infrared heat?

23.10.2017 | Automotive Engineering

3rd Symposium on Driving Simulation

23.10.2017 | Event News

VideoLinks
B2B-VideoLinks
More VideoLinks >>>