Every three seconds, someone in the world of dementia develops reason. Alzheimer’s disease is the most common form of dementia, which accounts for between 60 and 70 % of the total.
Although scientists have made significant progress in understanding the disease, there is still no cure. This is somewhat because Alzheimer’s disease has a variety of reasons – many of them have not yet been fully understood.
The two proteins, which are widely believed to play the main role in Alzheimer’s disease, are amyloid beta and tau. Amyloid forms the beta plaques in the outside of the brain cells. This disrupts the relationship between neurons. Tau accumulates inside the brain cells, where it wraps. This eventually leads to cell death. These plaques and spots are distinctive features of Alzheimer’s disease.
This understanding, known as the amyloid hypothesis, has formed research for decades and has led to treatments aimed at cleansing amyloid from the brain. Monoclonal antibody drugs have been confirmed in recent years.
But they only work in the early stages of the disease. They do not reverse existing damage and may cause serious side effects such as brain swelling and bleeding. Most importantly, they only target beta amyloid and do not cure tau.
But in a surprise twist, recent research published by my colleagues, and I found that a protein from Helicobacter pylori-bacteria, known for the cause of gastric ulcer-can cause both beta and tau amyloid to toxic. This unexpected finding may refer to a new strategy to combat Alzheimer’s disease.
Our discovery began with a very different question. We were initially studying how H Pylori interacts with other germs. Some bacteria form protective societies called biofilm, which rely on amyloid communities (similar to the plaque in the brain) as a structural scaffold. This surprised us: Can H Pylori interfere with human amyloid communities in humans, affect bacterial biofilms?
We turned our attention to a famous H Pylori protein called CAGA. While half of the protein is known that causes harmful effects on human cells (as the C-Terminal area), the other half (N-Terminal area) may have protective properties. Surprisingly, this piece of N-terminal, called Cagan, dramatically reduced the formation of both bacterial and biofilm amyloids in bacterial species Escherichia coli and pseudomonas.
Encouraging these results, we tested whether the same component of protein can block human beta amyloid proteins. To do this, we incolmed beta amyloid molecules in the laboratory: Some were treated with Kagan, while others remained normal. We then pursued amyloid formation using a fluorescence singer and an electron microscope.
We found that the samples treated during the test have much less amyloid formation. Even at very low concentrations, Kagan almost completely stopped beta from the formation of amyloid aggregates.
To understand how Kagan works, we used the nuclear magnetic resonance (which allows us to examine how the molecules interact) to examine how the protein interacts with beta amyloid. We also used computer modeling to check possible mechanisms. Noteworthy, Kagan also blocked the accumulation of Tau – indicates that it works on multiple toxic proteins involved in Alzheimer’s disease.
Blocking the disease
Our study has shown us that a piece of helicobacter pylori protein can effectively block the construction of two proteins that are involved in Alzheimer’s disease. This suggests that bacterial proteins – or subsequently modeled drugs – can one day block the first symptoms of Alzheimer’s.
In addition, these benefits may exceed Alzheimer’s disease.
In additional experiments, the same bacterial piece of IAPP (protein involved in type 2 diabetes) and Alpha Sinoklin (associated with Parkinson’s disease) blocked the same. All of these conditions are directed by the accumulation of toxic amyloid aggregates.
That a single piece of bacterial can interfere with many proteins shows exciting therapeutic potential. Although these conditions affect different parts of the body, they may be linked through the mutual dialogue between common amyloid-mucosanism that Kagan can help disorder.
Of course, this is clear: This research is still in the early stages.
All of our tests were done in laboratory settings, it was not yet in animals or humans. However, the findings open a new path.
Our study also revealed the essential mechanisms of how to block amyloid beta and tau of the formation of amyloid aggregates. One way to do this was to prevent proteins from collecting the masses. They also prevented the formation of small, early amyloid aggregates. In the future, we will continue to study the exact mechanism and evaluate the effects of animal models.
These results also raise one question: Can H Pylori, which has long been seen only as harmful, can also have a protective side? Some studies have pointed to the relationship between H. pylori infection and Alzheimer’s disease, although this relationship is still unclear. Our discovery adds a new layer to this discussion, indicating that part of H Pylori may actually interfere with the molecular events that lead to Alzheimer’s disease.
This means that in the future, we may need a more accurate and personal approach. Instead of eliminating H Pylori completely with antibiotics, it may be more important to understand it in various biological fields, which are parts of harmful bacteria, and may actually be useful.
Since the doctor continues to move more precisely, it may not be the other goal to destroy any germs, but to understand how some of them may work with us, not against us.
Gefei Chen is an assistant professor at Karolinska Institute.
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