Team members, Dr John Sanderson and Dr Paul Yeo from Durham University have helped produce the first ever, high-resolution, full-length structure of a protein from an enveloped virus called the 'matrix protein'.
Viruses work in many different ways but in this case, respiratory syncytial virus (RSV) virions form by a 'budding' process at the plasma membrane of a cell. The matrix protein appears to drive the final assembly process and the formation of viral filaments. It is also clear that the matrix protein is an important determinant of where the virus buds.
Using x-ray crystallography, the team's been able to see the intimate details of the matrix protein that controls how the RSV virus assembles inside a cell. The technique allows them to see how the virus protein functions and this could help the team to develop biochemical tools to treat respiratory ailments and the common cold.
Dr Yeo said: "We can now see what the protein virus structure looks like and we plan to pull the protein apart to see how and where it might be intercepted. These images provide amazing insights into the micro-chemical world of our cells. We have an opportunity to use bioactive chemistry to develop the medical tools of the future."
The team, funded by Durham University, the Wolfson Institute and One North East, looked at the matrix protein of respiratory syncytial virus (RSV), a virus which is the most dangerous respiratory virus affecting infants and for which there is no vaccine. About one in three people suffering a cold are affected by this particular enveloped virus. They are looking at the way in which the matrix protein pulls the virus together and assembles at the membrane of a cell. This interaction is crucial to the development of cellular disease.
Dr John Sanderson said; "Enveloped viruses can be extremely dangerous. They enter the cell and hijack its machinery. They assemble their own cell parts of proteins and nucleic acids, before pinching off a bit of the membrane lining of a cell, in this case the lung, and going on to infect new cells. Our new hi-resolution structure can help us to see how to disrupt that process."
Durham's researchers have looked closely at the different stages of virus assembly and replication and they are particularly interested at the stage where the virus assembles. It's at this stage that they intend to disrupt the protein.
Dr Paul Yeo said: "If you can intercept the virus at the right time, just before it exits the cell, then your immune system can deal with it. Almost all envelope viruses have to assemble and we want to see how the mechanism works, how the virus latches on to cells and how it buds inside them."
The researchers grew crystals of the protein, crystallised them, and then used x-ray diffraction to determine the position in space of every atom of the protein. The information was then used to create images of the protein's structure. These images enable the team see what different parts of the matrix protein do.
If scientists can understand how the protein binds to cell membranes, then chemists and biological scientists may be able to develop tools to stop the protein mechanism working; this could be a stepping stone to the development of drugs to fight viruses like RSV. The Durham team also hope to work on other viruses such as Hepatitis C and measles.
Dr Sanderson said: "The high-resolution and degree of crystallographic order that we've observed in the structure allows us to throw light on the way in which the membrane binds, and on the mechanism by which this protein performs its varied and critical roles. It's an exciting development that could help in the quest for the biochemical tools of the future."
The 5 stages of virus assembly and replication:Entry into the cell
Carl Stiansen | EurekAlert!
Scientists unlock ability to generate new sensory hair cells
22.02.2017 | Brigham and Women's Hospital
New insights into the information processing of motor neurons
22.02.2017 | Max Planck Florida Institute for Neuroscience
In the field of nanoscience, an international team of physicists with participants from Konstanz has achieved a breakthrough in understanding heat transport
Cells need to repair damaged DNA in our genes to prevent the development of cancer and other diseases. Our cells therefore activate and send “repair-proteins”...
The Fraunhofer IWS Dresden and Technische Universität Dresden inaugurated their jointly operated Center for Additive Manufacturing Dresden (AMCD) with a festive ceremony on February 7, 2017. Scientists from various disciplines perform research on materials, additive manufacturing processes and innovative technologies, which build up components in a layer by layer process. This technology opens up new horizons for component design and combinations of functions. For example during fabrication, electrical conductors and sensors are already able to be additively manufactured into components. They provide information about stress conditions of a product during operation.
The 3D-printing technology, or additive manufacturing as it is often called, has long made the step out of scientific research laboratories into industrial...
Nature does amazing things with limited design materials. Grass, for example, can support its own weight, resist strong wind loads, and recover after being...
Nanometer-scale magnetic perforated grids could create new possibilities for computing. Together with international colleagues, scientists from the Helmholtz Zentrum Dresden-Rossendorf (HZDR) have shown how a cobalt grid can be reliably programmed at room temperature. In addition they discovered that for every hole ("antidot") three magnetic states can be configured. The results have been published in the journal "Scientific Reports".
Physicist Dr. Rantej Bali from the HZDR, together with scientists from Singapore and Australia, designed a special grid structure in a thin layer of cobalt in...
13.02.2017 | Event News
10.02.2017 | Event News
09.02.2017 | Event News
22.02.2017 | Power and Electrical Engineering
22.02.2017 | Life Sciences
22.02.2017 | Physics and Astronomy