An important advance in understanding the structure of phage viruses, which infect and destroy bacteria, has been made by a team of scientists from Oxford and Finland, which could help develop new strategies to combat bacterial infections.
The results of a collaboration between research groups at Oxford University and the University of Helsinki, Finland, published in two articles in a recent edition of the journal Nature, describe the structural components of a phage virus, PRD1. It is the first time that a virus with a lipid membrane has been described in atomic detail using X-ray diffraction techniques.
In the Division of Structural Biology at the Wellcome Trust Centre for Human Genetics, the investigators involved analysed thousands of extremely fragile crystals of the virus PRD1, in order to collect enough data to solve its atomic structure. PRD1 is the largest biological macromolecular complex evervisualisedin atomic detail with over 30 different protein components. The virus has a biological membrane that for the first time has been described in three-dimensions using X-ray crystallography. The details in the structure reveal the mechanistic principles of how the virus is assembled. Comparison with other viruses reveals that these same principles areutilisedin several viruses infecting human cells. Research on these viruses helps scientists to plan strategies to combat bacterial infections using these deadly enemies of bacteria. This is of importance as antibiotic resistance is a growing concern with few alternatives to control bacterial infections in the future.
Image: A composite image showing the various components of the PRD1 virus, with the lipid membrane and associated proteins shown in green and red, and the outer surface shown in blue. Credit: Division of Structural Biology, Wellcome Trust Centre for Human Genetics.