Bacteria function strikingly similarly to human cells when it comes to defending against invaders, sharing the same essential machinery needed to turn immune pathways on and off. By examining these bacterial processes, we can learn much about how the human body functions. Jennifer Doudna, a biologist at the University of California, Berkeley, won the Nobel Prize in 2020 for her work on CRISPR. CRISPR which stands for Clustered Regularly Interspaced Short Palindromic Repeats, is a family of DNA sequences found in bacteria derived from DNA fragments of bacteriophages that had previously infected the bacteria. During successive infections, they are used to locate and eradicate DNA from bacteriophages that are similar to them. Scientific curiosity about the role proteins and enzymes play in the anti-phage immune response has been rekindled by the hype around CRISPR.
Read Also: A Novel Method Using “Soft” CRISPR May Provide a New Fix for Genetic Diseases
Much more than CRISPR
More CRISPR-like technologies are being brought to fruition in our world today. Growing evidence indicates that bacteria may have been the source of some components of the human immune system, with evolution leading to more sophisticated versions of bacterial virus-fighting mechanisms in both the plant and animal kingdoms. A group of scientists has conducted a study that has provided insight into the operation of a family of enzymes called ubiquitin transferases.
When a cell detects a viral intruder, cGAS (cyclic GMP-AMP synthase) is essential for mounting a downstream response in both bacteria and humans. Yet what controls this procedure in bacteria is unknown. They examined the structure of cGAS’ evolutionary forerunner in bacteria using cryo-electron microscopy and other genetic and biochemical tests. They found additional proteins that bacteria utilize to aid cGAS in protecting the cell from viral attack. They specifically found that bacteria alter their cGAS using a simplified “all-in-one version” of ubiquitin transferase, a complicated group of enzymes that in humans regulate immunological signals and other significant physiological functions. The study also identified proteins called Cap2 and Cap3 which regulate CGAS. It was shown that human ubiquitin can also act as a sort of marker for cellular waste, driving the breakdown and destruction of surplus or outdated proteins. Mutations can cause that mechanism to malfunction, leading to protein buildup and disorders like Parkinson’s disease.
Clinical significance
A deeper understanding of this enzyme, and perhaps even its reprogramming, could lead to the development of novel therapeutic strategies for a variety of human diseases. This ranges from autoimmune conditions like rheumatoid arthritis and Crohn’s disease to neurodegenerative conditions like Parkinson’s disease.
Conclusion
The scientists emphasize the need for more investigation, although the finding offers fascinating scientific doors. Parts of the bacterial ubiquitin transferase may one day be engineered to delete away problematic proteins and treat human disease.
Read Also: Study Shows That CRISPR-Edited T Cells for Cancer Treatment Are Safe and Long-Lasting
References
An E1–E2 fusion protein primes antiviral immune signalling in bacteria
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