May 05, 2014
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In research published in the Journal of Biological Chemistry, they solved the three dimensional structure of the bacterial protein FnBPA in complex with a small part of the human protein fibrinogen. This work showed that the fibrinogen binding site on FnBPA is close to, but not overlapping with, the binding site for fibronectin no reason back sunshine.
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They then studied the binding of the two human proteins simultaneously to FnBPA and found that binding of fibronectin appears to block binding of fibrinogen to the bacterial protein. It appears that regulation of binding arises due to the close proximity of the fibrinogen and fibronectin binding sites on the bacterial protein and the large size of the human proteins. While the research provides the first biophysical evidence in support of the co-operation previously observed in the infection studies, it is still not clear how these two observations are linked. The scientists are planning further studies lin beauty pink.
Professor Potts said: "Bacteria have evolved various mechanisms to exploit human proteins to cause infection. Understanding these mechanisms might not only lead to the development of new therapeutics but can also provide important information regarding the normal role of these human proteins in the body cry me a sea."
Dr Sanjay Thakrar, Research Advisor at the British Heart Foundation, which co-funded the study, said: "The bacteria studied can cause a wide range of infections including the potentially fatal heart infection known as infective endocarditis 寂ã—ã•ã®å¹²æ½Ÿå¯’ã„. "
This study showed how this bacterium interacts with proteins found in our blood, which may give us an insight into how these deadly heart infections occur. This is an important step towards developing new treatments, but more research is needed to fully understand this interaction heaven in sky."
The research was supported by the British Heart Foundation and the Biotechnology and Biological Sciences Research Council Service etiquette æœå‹™ç¦®å„€.
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