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Revised: June 7, 1998

How Bacteria May Cling to Tissues!

Scientists are coming closer to understanding how bacteria can resist antibiotics and cling to tissues in the body. A new breakthrough in the study of the helicobacter pylori, the bacteria that causes the great majority of ulcers in the United States, may shed light on infections in the body which, to the surprise of many, thrive in areas that research had thought would repel bacteria. Helicobacter Pylori lives in the extreme acid of the stomach and many an IC patient have wondered if another bacteria could live in the acid of the bladder. Below is the press release for this breakthrough, dated January 15, 1998.

Protein Allows Stomach Bug To Bind
NEW YORK (Reuters) -- A protein on the surface of the ulcer-causing bacteria Helicobacter pylori allows the organism to attach to the stomach lining and survive the highly acidic conditions of the stomach, scientists say.
The protein, blood group antigen-binding adhesin (BabA), may be used to formulate a vaccine that could prevent infection with the bacteria, according to a report in this week's issue of Science.
H. pylori infection greatly increases the risk of stomach inflammation or ulcer formation, and has been linked to a greater risk of stomach cancer.
About one third of US adults are infected with H. pylori, and 20% develop a peptic ulcer at some point in their lives. The rates of H. pylori can be much higher in some developing countries. While antibiotics can eradicate the bacteria, people can be reinfected and experts worry that the bacteria may become resistant to antibiotic treatment.
``There's a real need for new ways to prevent or cure H. pylori infection,'' said study co-author Dr. Douglas Berg in a statement released by Washington University in St. Louis, Missouri. A vaccine that boosts immunity to H. pylori ``...would be incredibly important,'' said Berg, a professor of molecular microbiology and genetics at the University.
The study was a collaborative effort between researchers at Umea University in Sweden; Washington University; University Hospital in Uppsala, Sweden; and Max-von Petten Kofer Institut fur Hygiene und Medizinsche Mikrobiologie in Munich, Germany.
Researchers have known for a number of years that the bacteria attach to the stomach by binding to two proteins, Lewis b (Le b) and H-1, which are found on cells of the stomach lining. But it wasn't clear how the bacteria accomplished the trick, once thought to be impossible. In the new study, the researchers isolated BabA by exposing H. pylori to Le b and purifying the protein that stuck to the molecule.
It's likely that this interaction ``plays a critical role in efficient delivery of bacterial virulence factors that damage host tissue either directly or through inflammatory or autoimmune reactions, eventually leading to ulcer disease,'' the authors wrote.
SOURCE: Science (1998;279:373-376)
Reut18:44 01-15-98
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