giovedì 20 febbraio 2014

How gut bacteria communicate within our bodies, build special relationship

http://feeds.feedburner.com/~r/sciencedaily/living_well/~4/QoC8yE2H8rA

Communication is vital to any successful relationship. Researchers from the Institute of Food Research and the University of East Anglia have discovered how the beneficial bacteria in our guts communicate with our own cells.This is a key step in understanding how our bodies maintain a close relationship with the population of gut bacteria that plays crucial roles in maintaining our health, fighting infection and digesting our food.A study, published in the journal Cell Reports, shows that the gut bacteria produce an enzyme that modifies signalling in cells lining the gut. The enzyme also has another role in breaking down food components.”Our study provides a breakthrough in understanding how bacteria communicate across different kingdoms to influence our own cells’ behavior, as well as how we digest our food,” said Dr Regis Stentz from the IFR, which is strategically funded by the Biotechnology and Biological Sciences Research Council.We all rely on trillions of bacteria in our gut to break down certain components of our diet. One example is phytate, the form phosphorus takes in cereals and vegetables. Broken down phytate is a source of vital nutrients, but in its undigested form it has detrimental properties. It binds to important minerals preventing them being taken up by the body, causing conditions like anemia, especially in developing countries. Phytate also leads to excess phosphorus leaching into the soil from farm animal waste, and feed supplements are used to minimize this.But despite the importance of phytate, we know very little about how it is broken down in our gut. To address this Dr Stentz and colleagues screened the genomes of hundreds of different species of gut bacteria. They found, in one of the most prominent gut bacteria species, an enzyme able to break down phytate. In collaboration with Norwich Research Park colleagues at the University of East Anglia, they crystallized this enzyme and solved its 3D structure. …


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