Groundbreaking research into some of the most deadly antibiotic-resistant diseases

Key points
- Pioneering research by a North East of England scientist could lead to a cure for some of the most deadly antibiotic-resistant diseases.
- Toxic Shock, Septicemia and the flesh-eating disease necrotizing faciitis are just some of the potentially fatal invasive infections caused by the streptococcus bacterium, which has increased significantly over the past 10 years.
- Until now, scientists have not understood what turns this ordinary bacterium - which is best known as the cause of sore throats - into something horrendous that can cause very invasive and potentially fatal diseases.
- Now, Dr Gary Black, and a team from Northumbria University's School of Applied Sciences, has isolated one of the main enzymes implicated in disease - known as a hyaluronidase, HylP1.
Pioneering research by a North East of England scientist could lead to a cure for some of the most deadly antibiotic-resistant diseases.
Toxic Shock, Septicemia and the flesh-eating disease necrotizing faciitis are just some of the potentially fatal invasive infections caused by the streptococcus bacterium, which has increased significantly over the past 10 years.
Until now, scientists have not understood what turns this ordinary bacterium - which is best known as the cause of sore throats - into something horrendous that can cause very invasive and potentially fatal diseases.
Now, Dr Gary Black, and a team from Northumbria University's School of Applied Sciences, has isolated one of the main enzymes implicated in disease - known as a hyaluronidase, HylP1. In a process similar to the one used in DNA testing, pure enzymes were produced in large quantities, by isolating the gene and then inserting it into a safe micro-organism for production.
Once the genes were cloned, the enzyme it produces, HylP1, was crystallised and then taken to the University of York - one of only a few UK centres specialising in structural biology - where Dr Black worked with scientists to solve the shape of the enzyme. There, he discovered its rare triple-stranded beta-helix shape, which is similar to only four other enzymes out of the thousands tested in recent years. He says:
"Solving the three dimensional structure of the enzyme means we have a better understanding of how the enzymes bind to other matter and how they work. We need to understand how the enzyme works to understand how we can stop it".
Dr Black's findings are published this week in Proceedings of the National Academy of Sciences of the United States of America (PNAS), one of the world's most cited multidisciplinary scientific serials. Set up in 1914, it publishes cutting-edge research and spans biological, physical and social sciences.
Dr Black now hopes one of the world's leading pharmaceutical companies will take up his research and use his findings to develop revolutionary life saving drugs. He says: "This is a major breakthrough which has the potential to save thousands of lives in the future."
Dr Black, 39, from County Durham, did a post-doctorate at Newcastle University and was a lecturer at Sunderland University before joining Northumbria University's School of Applied Sciences five years ago.
He started this pioneering research when he joined Northumbria and has been assisted by PhD student Anna-Marie Lindsay and the now qualified Dr Nicola Smith.
Professor John Ditch, Deputy Vice Chancellor (Research and Consultancy) at Northumbria University recognised the importance of this ground-breaking research when he awarded Dr Black a Promising Research Fellowship grant last year.
Written and revised by
David Cohen, M.D.
Our doctors write and review articles for accuracy and keep them up to date.
health.am provides general information, not medical advice. Always consult a qualified health professional about your own health.
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