Washington University scientists have unraveled the mystery of how Chlamydia bacteria bind to and infect host cells . The finding, reported in the current issue of Journal of Clinical Investigation , could open the door to find a cure for chlamydia, a sexually transmitted disease that affects more than 50 million people worldwide each year .
it is well known that Chlamydia trachomatis bacteria settles into its host by attaching to cells it infects, but Pathobiologist Cho-Chou Kuo and colleagues wanted to know more on its modus viruslike mode. There are more than a decade, Kuo had found evidence for a glycoprotein - a molecule consisting of a fused protein to a carbohydrate skeleton - which was part of the outer membrane of the bacterium. Kuo wanted to explain how this glycoprotein joined the host cell. Using a mapping technique developed in Japan, Kuo and his colleagues found an answer in isolating and identifying a carbohydrate present in very small quantities, it believes mediates Chlamydia "of the attachment to host cells.
The next step was to beat Chlamydia at his own game. By flooding potential host cells in vitro with a lure sugar before introducing Chlamydia bacteria in cells, Kuo said, "there was no place for Chlamydia to attach." As a result, the cells remain uninfected.
But blocking one sugar may not be the sweet solution Kuo plans. Gerald Byrne of the University of Wisconsin microbiologist, said that not everyone in the field believes that Chlamydia even glycoproteins, which are rarely found in bacteria. and there are other possible explanations of how Chlamydia interacts with host cells. However, Byrne believes that "there is no reason for the practical work can not continue. "
for the team of Kuo, then try to synthesize a carbohydrate that is equally effective but easier to work with than natural bait used in his experiments. Such carbohydrate may one day be added to contraceptive gel to help reduce the spread of Chlamydia . Although the gel would protect women, Kuo admits, "that's better than nothing."
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