Researchers examined the atomic structure of the ORF8 protein of the new coronavirus SARS-CoV-2, behind Covid-19 disease. The purpose of the structure is to evade and slow down the immune system’s response.
A team of scientists from the University of California, Berkeley, have identified the atomic structure of ORF8, a SARS-CoV-2 protein whose function is to help the pathogen ‘escape’ and delay the response of human immune cells.
The research was published in PNAS, showing the potential to enable new antiviral treatments adapted only for Covid-19.
“Using X-ray crystallography, we built an atomic model of ORF8, which highlighted two unique regions: one that is present only in SARS-CoV-2 and its immediate ancestor in bats and another that is absent from any other coronavirus,” explained study leader James Hurley in a press release.
“These regions stabilize the protein (which is a secreted protein, not membrane-bound as the peak proteins characteristic of the virus) and create new intermolecular interfaces. We, and others in the research community, believe that these interfaces are involved in reactions that somehow make SARS-CoV-2 more pathogenic than the strains it evolved from,” he added.
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According to scientists, the amino acid sequence of ORF8 is so distinct from any other protein that scientists had no reference to its shape, being the 3D form of a protein that dictates its function.
In the course of the research, the researchers gathered multiple methods of analysis and worked for more than six months in the laboratory until they achieved the feat.
As Galileo explains, the various types of coronaviruses undergo distinct mutations of viruses such as influenza or HIV, which quickly accumulate small changes through a process called hypermutation. However, in coronaviruses, huge blocks of nucleic acids often move through recombination and, and when it occurs, large and vast regions of proteins can appear.
Genetic tests carried out in the early days of the pandemic revealed that when the virus passed from bats to humans, a significant recombination mutation occurred in the sars-cov-2 genome zone encoding for the ORF7 protein, present in many coronaviruses.
ORF8, its new form, quickly aroused the interest of scientists around the world due to the fact that cases of significant genetic divergence such as the one found are often the reason for the virulence of a new strain.
According to Hurley: “basically, this mutation caused the protein to double in size, and the substance that doubled [in size] was not related to any known form.”
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“There is a nucleus of about half of the [protein] that is related to a type of format known in previous coronavirus structures, but the other half is completely new,” the expert concluded.