Neutralizing antibodies can be used to target the weakness, perhaps opening the door for therapies that would be equally effective for all variations.
Cryo-electron microscopy (cryo-EM) was employed in the study, which was published on Thursday in the journal Nature Communications, to disclose the atomic-level structure of the weak area on the virus’ spike protein, also known as an epitope or region to which an antibody attaches itself.
The SARS-CoV-2 virus enters and infects human cells using the spike protein. The researchers also provided details of an antibody fragment known as VH Ab6, which can bind to this location and neutralise every significant variation.
According to Sriram Subramaniam, a professor at the University of British Columbia and the study’s principal author, “”This is a highly adaptable virus that has evolved to evade most existing antibody treatments, as well as much of the immunity conferred by vaccines and natural infection”.
“This study reveals a weak spot that is largely unchanged across variants and can be neutralised by an antibody fragment. It sets the stage for the design of pan-variant treatments that could potentially help a lot of vulnerable people,” Subramaniam said.
Our bodies manufacture antibodies naturally to combat illness, but they can also be created in a lab and given to patients as a medication.
Despite the fact that a number of antibody therapies have been created for COVID-19, their efficacy has decreased in the face of severely mutated forms like Omicron.
“We have been looking for master keys — antibodies that continue to neutralise the virus even after extensive mutations,” he added.
The antibody fragment VH Ab6, which has been demonstrated to be effective against the Alpha, Beta, Gamma, Delta, Kappa, Epsilon, and Omicron variations, has been named by researchers as the “master key.”
By binding to the epitope on the spike protein and preventing the virus from entering human cells, the fragment neutralises SARS-CoV-2.
The team has been identifying vulnerable regions in each spike protein’s structural structure in an effort to develop new remedies.
The capabilities of the epitope described in this work are maintained across variants since it is largely absent from mutation hotspots, according to Subramaniam.
“Now that we have described the structure of this site in detail, it unlocks a whole new realm of treatment possibilities,” he said.
According to Subramaniam, drug manufacturers can now take advantage of this critical weakness. Because the region is largely mutation-free, the ensuing medicines may be effective against current and even foreseeable variants.