Three PhD students from the Institute of Food Research recently presented their work to an audience of MPs and leading scientists at The House of Commons. They were selected for the SET for Britain poster exhibition, organised by The Parliamentary and Scientific Committee. The aim of SET for Britain is to encourage, support and promote Britain’s early-stage and early-career research scientists, engineers and technologists who are the “engine-room” of continued progress in and development of UK research and R&D, and ultimately of UK plc.
Anthony Ash from the IFR is studying the salivary pellicle, a thin layer of proteins derived from saliva that covers our teeth and protects the enamel from damage by abrasion and acids in our food. He is trying to work out how the pellicle forms and what its physical and chemical structure is, which will help in the development of more effective oral hygiene products. Anthony is using the latest physical chemistry techniques to monitor and measure the salivary pellicle on surfaces, and see components in food or oral hygiene products affect how it forms or is broken down. This hasn’t been achieved before due to the technical difficulties in working with saliva, and the miniscule amounts of pellicle produced, so Anthony’s work will feed into the development of an accurate model of the complex salivary system.
Faye Jeffers is investigating how the bacteria that live in our guts are able to bind to the layer of mucus lining the wall of the gut. This attachment plays an important role in maintaining the balance, but surprisingly little is known about how it actually happens. Faye used strains of Lactobacillus reuteri to look for differences in their mucus binding ability. L. reuteri is a good model to study this as many different strains are commonly found colonising the guts of many vertebrates, including pigs, humans and mice. Twenty-five strains, from different host animals were tested to see which showed the highest level, and the genome of this strain was sequenced in collaboration with The Genome Analysis Centre, also on the Norwich Research Park. This highlighted a mucus binding protein not seen in other strains, and also showed that the mucus binding is strain specific.
Emma Meader has been looking at a new way of preventing Clostridium difficille infection, the leading cause of hospital-acquired diarrhoea. C. difficile is carried by up to 10% of the population as part of their normal flora, but disruption of this balance, (often as a result of antibiotic therapy) permits rapid growth and the production of potent toxins that give rise to diarrhoea and stomach cramps, and in severe cases toxic megacolon and death. Using the colon model, Emma has shown that bacteriophages (viruses that infect bacteria, but not humans), can reduce levels of C. difficile and suppress the production of toxins. Bacteriophages were discovered in 1915 and have been used therapeutically in countries including Georgia and Poland ever since. In the West there is now renewed interest in bacteriophage therapy owing to the increasing levels of antibiotic resistance, and Emma’s study has demonstrated some of the advantages and challenges that this method of treatment can offer.
A fouth representative from the Norwich Research Park was Alaa Aljabali from the John Innes Centre, who is working in the area of nanotechnology for delivering drugs. He is looking to use empty virus-like particles (eVLPs) derived from the Cowpea Mosaic Virus as a way of targeting the delivery of drugs. The idea is that a therapeutic could be encapsulated in the eVLP, and the surface of the particle can be further modified with molecules that direct the particle to the diseased cell.