A previously unrecognized molecular structure on the surface of the human bacterial pathogen Group B Streptococcus (GBS) – the most common cause of sepsis and meningitis in newborn infants – is described by researchers at the University of California, San Diego (UCSD) School of Medicine in Proceedings of the National Academy of Sciences published online the week of July 19, 2004.
The new discovery has important implications for understanding the mechanism of infection and the design of vaccines to boost human immunity against this potentially devastating pathogen. For example, potential GBS vaccines currently in clinical trials have been developed without this new knowledge, which could possibly impact their effectiveness.
The findings are a collaborative effort between the laboratories of senior author Ajit Varki, M.D., UCSD professor of medicine and cellular and molecular medicine, and co-director of the UCSD Glycobiology Research and Training Center (GRTC), and Victor Nizet, M.D., associate professor of pediatrics, UCSD Division of Infectious Diseases and an attending physician at Children’s Hospital, San Diego. The two groups have been studying the phenomenon in which certain bacterial pathogens coat their surfaces with a thick capsule made of carbohydrate sugars similar to those found on the surface of human cells. In the case of GBS, the bacterial surface capsule contains sialic acid, a sugar that is also displayed prominently on the surface of all cells in the human body. It is believed that GBS uses sialic acid as a form of “molecular mimicry”, where the bacteria disguises itself to look more like human cells and thereby avoids recognition by the immune system.
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Many pathogens use certain sugar compounds from their host to help conceal themselves against the immune system. Scientists at the University of Bonn have now, in cooperation with researchers at the University of York in the United Kingdom, analyzed the dynamics of a bacterial molecule that is involved in this process. They demonstrate that the protein grabs onto the sugar molecule with a Pac Man-like chewing motion and holds it until it can be used. Their results could help design therapeutics that could make the protein poorer at grabbing and holding and hence compromise the pathogen in the host. The study has now been published in “Biophysical Journal”.
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