Feb. 24, 2009 Prof Dave Stuart, Director of Life Sciences at Diamond – the UK national synchrotron – and head of the Structural Biology Laboratory at Oxford's Wellcome Trust Centre for Human Genetics will unveil the structure of a biological protein from the vaccinia virus at the American Association for the Advancement of Science – AAAS- in Chicago. This is a significant step towards unlocking effective therapies to treat viruses.
The structure was solved at Diamond by Prof Stuart and his colleagues in December 2008 when they discovered that this complicated member of the poxvirus family is related to a large number of simpler viruses and shows the relevance of Darwinism to these, the simplest form of life.
Prof Stuart explains the significance of the new findings, "Viruses are by their very nature extremely hard to classify. They are much more common and diverse than any other form of life. On top of this, they evolve about 1 million times quicker than animals and we have no fossils to help us track their evolution back through history. Determining the structure of proteins is our best approximation to a fossil record and knowing more about virus families and the relationships between these families will help us to develop new, more effective, therapies".
The evolutionary path of human beings and animals fascinated Darwin and the quest for knowledge in this complex research area continues in the 21st century through the complex studies of many structural biologists across the world.
Prof Stuart continues, "With these latest results, we have been able to confirm our theories about the vaccinia virus at Diamond. This is a step towards a reclassification of the virus world, which can guide the way we think about therapies in the future. Currently, with viruses such as HIV, the therapies are targeting the replication machinery of the virus rather than their shells. If structural commonalities between viruses are known, these links can be used to create therapies that work on a family of viruses, as opposed to just one. With this approach, it is possible that we could be able to treat patients who are suffering from one of a number of viruses, in the same way that antibiotics are used to treat bacterial infections."
A combination of globalization, changes in agricultural practices, and the ecology of the planet pose problems in terms of virus outbreaks and pandemics. However, the growth of the international synchrotron community over the past 30 years means that there are now around 50 science facilities where biological protein structures can be studied and solved, offering the potential for a fast global response to new virus outbreaks. Synchrotrons have already played a crucial role in the advancement of modern structural biology. There are currently over 50,000 protein structures published in the Protein Data Bank and around 7,000 are being added each year, 95% of these are as a result of experiments that take place at synchrotron science facilities.
Prof Stuart has himself spent many hours working at synchrotrons around the world. One of the UK's leading structural biologists, he is particularly interested in the study of human and animal viruses – their structure, how they interact with host cells and the mechanisms by which they elicit a response to infection in the body. He has determined the structure of the foot-and-mouth disease virus, the blue tongue virus and more recently a membrane enveloped virus. He is also interested in the structure of the human immunodeficiency virus (HIV) and has published the structures of several of the viral components which have led to insights into the assembly of HIV and how it replicates inside cells.
In addition to his own research Prof Stuart praised the achievements made by many structural biology groups in the UK over the past year, and in particular, the work of Prof. Rick Lewis and his colleagues at Newcastle University who in the past 15 months alone have solved 8 de novo protein structures using Diamond – real success given that solving de novo protein structure is notoriously difficult and requires vast computational resources.
Rick Lewis, Professor of Structural Biology at the Institute for Cell and Molecular Biosciences at Newcastle University concludes: "It has been an exciting time for the team at Newcastle and our access to Diamond is integral to our goals to understand the molecular mechanisms behind DNA replication; the construction of the cell wall of bacteria, and how bacteria recognise and respond to harmful changes in their environments."
Other social bookmarking and sharing tools:
Note: Materials may be edited for content and length. For further information, please contact the source cited above.
Note: If no author is given, the source is cited instead.