A BREAKTHROUGH by bacteriologists in Scotland is paving the way to new treatments for killer respiratory infections such as pneumonia.
Scientists from St Andrews University and Oxfordshire-based Diamond Light Source have unravelled the structure of a key enzyme in Streptococcus pneumoniae, the bacteria responsible for infections including pneumonia, meningitis, and septicaemia.
The findings are published in the Journal of Biological Chemistry.
Respiratory infections are one of the biggest killers in the western world, particularly among children and the elderly.
Researchers used intense beams of light to uncover the structure of NanC, a type of enzyme known as a neuraminidase. Streptococcus pneumoniae bacteria contain up to three neuraminidase enzymes: Nan A, B and C.
The scientists had already uncovered the structure of the other two neuraminidases – A and B. The discovery of the NanC structure is the final step in identifying how these enzymes work to sustain S. pneumoniae, and how they could be targeted and disabled to destroy the bacteria.
Martin Walsh, deputy life sciences director at Diamond and lead author on the study, said:
“With the structure of NanC, we now have a vital new piece of the puzzle which informs wider research into drug design and equips us to better tackle the pneumococcus in all its forms."
Garry Taylor, Professor of Molecular Biophysics and Deputy Principal of St Andrews University, said: “With a fuller understanding of the structure and function of S. pnemoniae’s three neuraminidase enzymes, we’re now better equipped to design next-generation antibiotics for some of the world’s most prevalent and deadly respiratory infections.”
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