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A look at the atomic structure: What makes viral variants successful

A look at the atomic structure: What makes viral variants successful

A look at the atomic structure
What makes virus variants successful

Mutations can allow the coronavirus to evade part of the immune response produced naturally or by vaccination. A new study shows how these escape mutations work.

It is still not entirely clear which mutations in the coronavirus could be particularly dangerous and why. Especially with regard to whether the mutations have been picked up by the immune response to vaccines developed to date, it is expected that new results will be discovered urgently. In search of answers, researchers have now penetrated the atomic structure of the mutated virus with high-precision tools and uncovered the “success secrets” of the mutations.

In your A study published in the research journal “Science”. Researchers on Ian Wilson of the Scripps Research Institute in La Jolla / California focused on three mutations in the Sars-CoV-2 spike protein: K417N, E484K, and N501Y. These mutations can be found alone or in combination in most of the important Sars-CoV-2 variants. All mutations are located at the Sars CoV-2 receptor binding site, where the virus binds to the host cells.

This enabled the researchers to see how the mutations affect the sites that the antibodies can bind to and neutralize the virus. According to scientists, this explains, among other things, how variable B.1.1.7 was able to displace the wild type D614G in western countries. The mutation, first detected in December in the Kent region of England, owes its success, according to the results of the study, to the strongest association with the ACE2 receptor. Previous studies have already shown an increase in infection. Presumably, the stronger attachment makes it easier for the virus to enter cells. According to experts, this also allows the virus to replicate more quickly with mutations To explain.

The boom is not exhaustive

On the other hand, B.1.351, also known as the South African variant, and P.1 (Brazilian variant) with mutations E484K and K417N, are likely out of reach of the antibody. The researchers tested representative antibodies from key classes that target the general region in and around the receptor binding site. They found that many of these antibodies lose their ability to effectively bind to the virus and neutralize it if mutations are present. Both viruses also contain the N501Y mutation, which strengthens the bond compared to the wild type.

However, in some ways, researchers can provide all clarity to mutations. to me An advertisement from the Scripps Research Institute It can be shown that the three most important viral mutations do not alter other vulnerable parts of the virus outside of the receptor binding site. The antiviral neutralizing antibodies targeting the other two regions outside the receptor binding site remained largely unaffected by the three mutations examined. According to the scientists, their findings provide clues to future vaccines or treatments that may offer broader protection against the variants.