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New therapies to protect against COVID-19 are constantly being researched. But with a virus which presents itself with new variants almost every few months, finding the best level of protection has been futile. Antibody therapy however, has provided startling results in the fight against COVID-19, according to a new study.
The virus that causes COVID-19 today is not the same as the one that first struck our lives back in early 2021.
Experts warn that many of the variants circulating now are worryingly resistant to some of the antibody-based therapeutics which were developed for a different type of virus.
Many of the variants circulating now are partially resistant to some of the antibody-based therapeutics that were developed based on the original virus.
As the pandemic continues, more variants inevitably will arise, and the problem of resistance will only grow.
Finding a therapy which is highly protective against a wide range of viral variants is on the forefront of most medical researchers.
An antibody may have been identified that is highly protective at low doses by researchers at Washington University School of Medicine.
Moreover, the antibody attaches to a part of the virus that differs little across the variants, meaning that it is unlikely for resistance to arise at this spot.
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The study has been published in the journal Immunity and could be a step toward developing new anti-body-based therapies which are less likely to have their potency reduced even with virus mutations.
Senior author, Dr Michael Diamond said: “Current antibodies may work against some but not all variants.
“The virus will likely continue to evolve over time and space.
“Having broadly neutralising, effective antibodies that work individually and can be paired to make new combinations will likely prevent resistance.”
To find neutralising antibodies that work against a wide range of variants, the researchers began by immunising mice with a key part of the spike protein known as the receptor-binding domain.
Then, they extracted antibody-producing cells and obtained 43 antibodies from them that recognise the receptor-binding domain.
The researchers screened the 43 antibodies by measuring how well they prevented the original variant of SARS-CoV-2 from infecting cells in a dish.
The researchers selected the two antibodies that were most effective at protecting mice from disease and tested them against a panel of viral variants.
The panel comprised viruses with spike proteins representing all four variants of concern (alpha, beta, gamma and delta), two variants of interest (kappa and iota), and several unnamed variants that are being monitored as potential threats.
“This antibody is both highly neutralising (meaning it works very well at low concentrations) and broadly neutralising (meaning it works against all variants),” added Dr Diamond.
“That’s an unusual and very desirable combination for an antibody.
“Also, it binds to a unique spot on the spike protein that isn’t targeted by other antibodies under development.
“That’s great for combination therapy. We could start thinking about combining this antibody with another one that binds somewhere else to create a combination therapy that would be very difficult for the virus to resist.”
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