Professor Martin Steineger’s research team at Seoul National University announced the results of a study showing that many of the human immune-related proteins have a three-dimensional shape similar to the proteins found in bacteria. The photo shows a bacterial protein (A0A1C5UEQ5) with a structure similar to that of a human immune-related protein (O14862). /Seoul National University
Research has shown that many of human immune-related proteins have a three-dimensional shape similar to proteins found in bacteria. A Seoul National University research team compared the structures of hundreds of millions of proteins and discovered a protein group that had not been studied until now. There are expectations that new discoveries in human immune function will have a positive impact on the fields of evolutionary biology and medicine.
Professor Martin Steineger’s research team in the Department of Life Sciences at Seoul National University, in collaboration with ETH Zurich and the European Bioinformatics Institute (EMBL-EBI), announced on the 14th that they had found a link between human immune-related proteins and bacterial proteins. After comparing the structures of hundreds of millions of proteins, the research team found that many of the human immune-related proteins had a three-dimensional shape similar to that of proteins found in bacteria. Similarities were discovered between previously unknown human proteins involved in the immune system and proteins found in bacterial species.
Proteins act as a kind of ‘molecular machine’ that constructs and operates cells. Proteins are made of amino acid chains, like a bracelet made of colorful beads, and are then folded into a three-dimensional structure to perform their function. It is known that there are over 200 million proteins in all biological species, and humans have genetic information for about 20,000 proteins.
Protein analysis has been considered important in the scientific community because information about protein function and evolution is closely related to life phenomena. However, with existing technology, it took more than 10 years to cluster 200 million protein structure data (analysis of dividing data into groups with similar characteristics). To solve this inconvenience, Professor Steineger’s research team developed an algorithm called Foldseek Cluster last May to reduce protein structure search time. Using the FoldSearch cluster, a protein structure search that used to take several months can be completed in 5 days.
Proteins form a stable three-dimensional structure by folding amino acid chains, and FoldSearch speeds up the search by expressing the three-dimensional structure as a single sequence. This time, thanks to FoldSeek technology, we were able to find that the structures of human immune-related proteins and proteins found in bacteria are similar.
“We found that many of the human immune-related proteins have a three-dimensional shape similar to proteins found in bacteria,” said Professor Steineger. “This suggests that our immune system differentiates from proteins that are much older than previously assumed. “It suggests that it may have happened,” he said.
Co-researcher Professor Pedro Beltrao of the University of Zurich said, “This study is like discovering a kind of time machine for evolutionary history that can look back on when and how proteins began to differentiate in the distant past.”
The results of this study were published today in the international academic journal Nature.
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2023-09-13 15:00:00
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