Recently, researchers who keep tabs on new COVID-19 variants noticed a trend that many are carrying the same set of three mutations.
A Phys.org report said that researchers investigated how the mutations change the way key pieces of the virus function in a new study.
Like storm waves that batter a ship, new versions of the COVID-19 virus have buffeted the world.
Their studies reveal how the three change the traits they need to cause and sustain infection of COVID-19.
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Triple Mutation
Essentially, the virus SARS-CoV-2 has caused human cells to replicate its genetic code countless times over the last couple of years, and, in the process, errors have arisen.
Such errors, also known as the mutations, are the new variants' raw materials. Scientists have discovered that almost half of these genetic sequences within variants comprise three mutations at positions known as K417, E484, and N501.
All alterations are tweaking the same part of the virus, also called the "receptor binding domain." This enables SARS-CoV-2 to infect human cells by locking onto their ACE2 protein.
The widespread existence of this combination has suggested that together, the said mutations offer the virus benefits not plausible with a single alteration.
Effects of the Mutations on Cells
In this study published in the Biochemistry journal, Vaibhav Upadhyay, Krishna Mallela, and colleagues wanted to tease out the benefits and drawbacks of each of the three mutations individually in combination.
As an initial step, the study authors generated domains that continued the mutations and studied their impacts on cells grown in Petri dishes.
The research team investigated how well cells could yield the domain, the stability of the domain, its ability to bind to ACE2, and the ability to escape antibodies.
The study findings revealed that every mutation enhances at least one of the characteristics, although at a cost. For instance, the K417 change increased the domain's production and stability, which improved its ability to evade a certain type of ability.
Evading 2 Antibody Types
The said change increased the domain's ability to attach to ACE2. The other two mutations were found to have different strengths and weaknesses, a similar Mirage News report specified.
Nonetheless, they were all put together; the changes mitigated the adverse effects of one another. Domains with all three mutations could bind ACE2 tightly and evade two types of antibodies, yet were also produced at the same levels as the origins virus and were just as stable.
By revealing the details of the manner natural selection can favor the mixture of mutations, these results provide a new understanding of the evolution of the virus, the researchers specified in this new study.
Related information about COVID-19 mutations is shown on Yale's School of Medicine's YouTube video below:
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