Researchers Discover Peptides Produced by Proteasome for Protein Degradation


Scientists at the Max Planck Institute for Multidisciplinary Sciences have made a significant breakthrough in understanding protein degradation by the proteasome, a waste system in living cells. The research team, led by Juliane Liepe, simulated protein degradation in the laboratory and identified and quantified the peptides produced. This discovery could have implications for predicting immunopeptides and developing new vaccines for infectious diseases and cancer.

The proteasome in living cells acts as a cellular recycling plant, breaking down proteins that are no longer needed or defective. The resulting peptides serve as components for new proteins or act as signal flags for the immune system by being brought to the cell’s surface. Immune cells can recognize and distinguish between healthy cells and those infected with viruses or cancerous cells based on these peptides. Consequently, the immune system can destroy infected or cancer cells.

The proteasome not only breaks down proteins into smaller peptides but can also reassemble them through a process called peptide splicing. Liepe’s research group is particularly interested in studying spliced peptides and their contribution to immune defense. By understanding the specific peptides generated by the proteasome, the team hopes to utilize them for immunotherapies in the future.

To gain insights into peptide splicing, the researchers conducted lab experiments that demonstrated how the proteasome degrades proteins. They also utilized computational methods, including machine learning, and developed new computer programs to identify and quantify different types of peptides.

The research team collaborated closely with scientists from the Francis Crick Institute and King’s College London in the United Kingdom, the National University of Singapore, and other teams to generate the largest known data set of peptides produced by the proteasome under laboratory conditions.

Through their experiments and analysis, the scientists uncovered several key findings. They found that the proteasome has preferences for specific sequences of protein components, leading to specific areas of proteins being processed more frequently. Additionally, they identified clear features that distinguish spliced from non-spliced peptides.

The researchers believe that their findings can lead to improved predictions of peptide splicing by the proteasome. This, in turn, could facilitate the development of novel vaccines against cancer and infectious diseases.

Juliane Liepe emphasizes the significance of their discoveries, stating that understanding how the proteasome produces immunopeptides allows for the prediction of peptide splicing, which can ultimately drive the development of new vaccines. This research opens up new possibilities for immunotherapies and has the potential to make significant strides in the prevention and treatment of various diseases.

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