According to the team’s research, published in the Proceedings of the National Academy of Sciences
, H. pylori
uses a unique biosynthetic pathway to synthesize vitamin K2. In humans, this vitamin plays a role in blood clotting; for the bacterium, on the other hand, it is essential to many vital chemical reactions that keep the organism alive. Interfering with the aforementioned pathway could weaken or even kill the bacteria. The enzyme HpMTAN (H
5′-methylthioadenosine nucleosidase) operates in that unique pathway and, according to movements the researchers predicted using Oak Ridge’s High Flux Isotope Reactor (HFIR), could, if targeted by a treatment, be prevented from aiding and expediting crucial reactions in the bacterial system, thereby killing the organism. The HFIR visuals enabled the researchers to observe how HpMTAN positions itself when it binds to other materials (substrates), which will allow researchers to target the enzyme and its associated reactions with medications.
Donald Ronning, PhD, a professor of biochemistry at the University of Toledo and leader of the research team, wrote that the new information “will inform future drug design efforts.” He added that this would likely take several years, but that his team’s efforts could expedite treatment development for H. pylori
that would not, unlike currently available treatment options, eliminate all gastric bacteria.
is infectious, but the exact route of transmission is not known for sure. The CDC suggests that either hand-to-mouth or mouth-to-mouth transmission of contaminated fecal matter may be the most common routes of transmission. The CDC recommends that any patient with “active gastric or duodenal ulcers or a documented history of ulcers” be tested.
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