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Spike protein mutations help Omicron escape antibodies

To understand why the Omicron variant (B.1.1.529) of the SARS-CoV-2 coronavirus is more infectious and transmissible, an international team of scientists investigated the mutations present in the spike protein (S). It is through it that the covid-19 virus can invade healthy cells in the body.

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Published in the journal Science , the study involved the participation of different research centers such as the Howard Hughes Medical Institute and the University of Washington. According to the authors, mutations in the spike protein allow the virus to escape antibodies developed against other coronavirus variants and also be able to invade healthy cells more quickly.

Omicron mutations increase the risk of reinfection and facilitate the escape of antibodies (Image: Reproduction/Veesler et al., 2022/Science)

"The findings provide a blueprint that researchers can use to design new protective measures, such as vaccines or therapy, against Omicron and other coronavirus variants that may emerge," said University of Washington scientist David Veesler.


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“This virus has incredible plasticity: it can change a lot and still maintain all the functions it needs to infect and replicate,” Veesler said of the mutations. "And it's almost guaranteed that Ômicron is not the last variant we'll see," he added.

Omicron mutations

It is worth remembering that the Ômicron variant was first identified in November 2021 in South Africa and, since then, the global numbers of cases of the new strain have not stopped growing. In addition to being highly infectious, the variant is able to "escape" more easily from antibodies produced against previous variants, which can lead to people already infected to reinfect themselves and reduce the protection of vaccines.

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According to the researchers, one of the reasons for the high transmissibility is the large number of mutations in the amino acid sequences of the spike protein of the coronavirus. To be more precise, there are 37. These directly affect the area known as the Receiver Binding Domain (RBD).

RBD is the target of the ACE2 enzyme, present in human cells and the gateway to the coronavirus. The research concluded that these mutations were responsible for increasing the ability of RBD to bind ACE2 by up to 2.4 times.

In addition, the team observed that the mutations altered the way the spike protein interacts with antibodies. For example, the ability of almost all monoclonal antibodies against it is reduced.

Now, the aim of further research on the SARS-CoV-2 coronavirus will be to identify additional regions in the spike protein that are at lower risk of mutating and are more stable. This will allow vaccines, in the future, to trigger a strong and lasting immune response against numerous variants.

Read the article on Canaltech.

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