The antibody found is capable of binding to the most stable region in the structure of the S-protein of the coronavirus that remains relatively unchanged throughout the development of SARS-COV-2 in the body.

SARS-CoV-2, a novel coronavirus, has caused more than 256.48 million infections and 5.14 million deaths.

Despite the development of an extraordinary number of COVID-19 vaccines and neutralizing mAbs in the last year, a key concern is the emergence of more transmissible and/or immune evasive SARS-CoV-2 VOCs, which are antigenically unique and become dominant in COVID-19 prevalence over time.

Now, a team of Chinese molecular biologists have identified the 35B5 antibody, which can bind to the most stable region of the coronavirus’s S-protein structure and neutralize all strains, including the omicron.

A unique antibody was found in a blood sample of one of the recovered residents of China.

In its further tests, mAb 35B5 protected all rodents from death and serious damage to the lungs.

The versatility of the molecule is that it binds to that part of the S-protein of the coronavirus, which hardly changes during the evolution of SARS-CoV-2. 

“35B5 neutralizes SARS-CoV-2 by targeting a unique epitope that avoids the prevailing mutation sites on RBD identified in circulating VOCs, providing the molecular basis for its pan-neutralizing efficacy,” the scientists write.

They further write: “the 35B5-binding epitope could also be exploited for the rational design of a universal SARS-CoV-2 vaccine.”

The study was published in the preprint server bioxiv*.

*Important Note:

Preprints are uncertified reports of work that have not gone through peer review. They shouldn’t be used to guide clinical practice or health-related behavior, and they shouldn’t be published as fact in the news.

Source: bioxiv

Image Credit: AP

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