The dozens of mutations found in the spike protein of the Omicron variant help it to evade all four classes of antibodies that can target the SARS-CoV-2 virus that causes COVID-19, suggests a study.

According to Sasisekharan, the traditional approach of only examining changes in the virus' genetic sequence reduces the complexity of the spike protein's three-dimensional surface and doesn't describe the multidimensional complexity of the protein surfaces that antibodies are attempting to bind to.

"It is important to get a more comprehensive picture of the many mutations seen in Omicron, especially in the context of the spike protein, given that the spike protein is vital for the virus's function, and all the major vaccines are based on that protein," he said.

Even though Omicron is able to evade most antibodies to some degree, vaccines still offer protection, Sasisekharan said.

"What's good about vaccines is they don't just generate B cells, which produce the monoclonal [antibody] response, but also T cells, which provide additional forms of protection," he said.

The team focused their analysis on the receptor-binding domain (RBD), which is the part of the spike protein targeted by antibodies.

Using their network modeling approach, the researchers studied how each of the mutations on the RBD changes the protein's shape and affects its interactions with four classes of human antibodies that target SARS-CoV-2.

Class 1 and 2 antibodies target the RBD site that binds to the Angiotensin-converting enzyme 2 (ACE2) receptor while class 3 and 4 antibodies bind to other parts of the RBD.

The researchers compared the Omicron variant to the original SARS-CoV-2 virus, as well as the Beta and Delta variants.

The findings from the new study could help to identify regions of the RBD that could be targeted with future vaccines and therapeutic antibodies.

(This story was published from a syndicated feed. Only the headline and picture have been edited by FIT.)