While the bacterium Streptococcus pneumoniae is found in 10-40 per cent of healthy people with no ill effects, it is the cause of common diseases including pneunomia, meningitis, and ear infections. Unfortunately, more and more penicillin-resistant strains of S. pneumonia are becoming prevalent, and these strains are also developing resistance to other antibiotics. There are still a few antibiotics available to treat S. pneumoniae, but resistance to these drugs will also certainly emerge. New, more effective ways to treat bacterial infections are urgently required. Bacteria have adapted the ability to use different carbohydrates, or sugars, for a number of biological processes such as metabolism. S. pneumoniae has a number of protein enzymes devoted to carbohydrate metabolism, including a pathway dedicated to degrading (breaking down) the sugar fucose. Certain proteins in this pathway have been found to be important in some aspect of S. pneumoniae infection and disease. Melanie Higgins is focusing her research on a protein called GH98. GH98 is found on the outside of the bacteria and is thought to be the first step in this fucose degradation pathway. In order to better understand how this enzyme works, Higgins will first determine the three-dimensional structure of GH98. From these structures, she will develop synthetic inhibitor molecules that keep GH98 from functioning. Her work will answer whether S. pneumoniae can still infect host cells and spread disease in the absence of GH98. If these inhibitors are proven effective, they could become a novel treatment for S. pneumoniae infections, providing clinicians more options for treating a number of bacterial diseases.