The findings also could help explain why the stomach inflammation that often accompanies the infection periodically flares up, then subsides, and why the infection persists for so long, says Berg, who also is a member of the tumor immunology program at the Alvin J. Siteman Cancer Center at Barnes-Jewish Hospital and Washington University School of Medicine.
"The ability of Helicobacter pylori to adjust its adherence properties to the level of inflammation it causes at the stomach surface could help explain how this bacterium maintains its persistent, decades-long infection in the stomach of millions worldwide," says lead investigator Thomas Born, D.D.S., Ph.D., assistant professor of odontology and oral microbiology, at Ume University, Ume, Sweden.
H. pylori colonizes the stomach of more than half of all people worldwide. Scientists believe the infection starts in infancy and lasts for decades, perhaps for a lifetime. Adherence to the epithelial cells that line the stomach is thought essential for the infection to occur. There's been a long-standing effort to find the molecules that H. pylori recognizes on stomach cells and to find the corresponding adhesins that it makes to recognize those host molecules.
In 1993, Born, working in collaboration with researchers at Washington University, learned that H. pylori used a molecule known as Lewis B antigen (Leb) to adhere to stomach cells, findings that also were published in Science. This study was followed up in 1998 when Born's team, working in collaboration with Berg and other investigators at Washington University, identified the attachment protein used by the bacterim, calling it Lewis B antigen binding adhesin (BabA). That discovery also appeared in Science.
The present study began with the intriguing observation that a mutant H. pylori strain engineered to lack Ba
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Contact: Darrell E. Ward
wardd@msnotes.wustl.edu
314-286-0122
Washington University School of Medicine
25-Jul-2002