Scientists have used the UK’s synchrotron science facility, Diamond Light Source, to solve the structure of a key enzyme in Streptococcus pneumonia (the pneumococcus). These bacteria cause a range of respiratory infections, including sinusitis, bronchitis, ear infections, pneumonia, meningitis and septicaemia.
Respiratory infections are one of the biggest killers in the western world, and pneumococcal infections can range from mild to potentially deadly. Children and older people are most at risk, as well as those with compromised immune systems.
Scientists from Diamond and the University of St Andrews have used crystallographic techniques on the synchrotron’s MX beamlines to uncover the structure of NanC, a type of enzyme known as a ‘neuraminidase’. These enzymes help the bacteria to grow and spread and are an important target for future antibiotics.
S. pneumoniae bacteria contain up to three neuraminidase enzymes, Nan A, B and C. The scientists have already uncovered the structure of the other two neuraminidases – A and B – and 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, thus destroying the bacteria.
Martin Walsh is deputy life sciences director at Diamond and lead author on the study. He comments: “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. The next step will be for scientists to use this structural information to aid in the design of inhibitors of the pneumococcus neuraminidases which could lead to new treatments for pneumococcal disease.”