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The number of people infected with the coronavirus in the world has already exceeded one million cases. There is a kind of race among scientists and research companies – who will be the first to know the virus so that it will be able to produce a vaccine and develop an effective treatment. A new study has revealed a potential “Achilles heel” of SARS-CoV-2.
SARS-CoV-2 sensitive to anti-SARS-CoV antibodies
According to a study by scientists at Scripps Reasearch, an antibody obtained from a survivor of the SARS epidemic in early 2002 revealed a potential vulnerability of the SARS-CoV-2 coronavirus.
The SARS-CoV and SARS-CoV-2 coronaviruses are genetically related. Scientists want to use this similarity. They mapped the interaction of a SARS-CoV antibody taken from a survivor of SARS infection with the new SARS-CoV-2 coronavirus. Although the antibody was produced in response to SARS infection, it cross-reacts with the novel SARS-CoV-2 coronavirus.
Structural mapping revealed nearly identical sites in both coronaviruses to which a given antibody binds, thus suggesting that it is an important and vulnerable site for this type of coronavirus.
“Knowing these protected sites could aid in the design of vaccines and therapeutic agents against SARS-CoV-2 that would also protect against other coronaviruses – including those that may emerge in the future,” explains study senior author Ian Wilson, professor of structural biology and head of the Department of Integrative Structural and Computational Biology at Scripps Reaserch.
The ultimate goal of the research is to obtain structural information about antibodies and their binding sites and use them to develop a SARS-CoV-2 vaccine design.
SARS-CoV-2 Achilles heel – binding site with the CR3022 antibody
The antibody that the entire study is focusing on is called CR3022 and was originally isolated in 2006 by the pharmaceutical company Crucell Holland BV in the Netherlands. Chinese scientists indicated that the antibody cross-reacts against SARS-CoV-2.
The team of researchers at Scripps Research used this research and knowledge of structural mapping to determine how the antibody binds to the SARS-CoV-2 coronavirus. Key was the discovery that the antibody binding site is very similar between the two coronaviruses – it differs by only four amino acids.
types of proteins secreted by plasma cells (B lymphocytes) in the course of a humoral immune response. They are part of the immune system and play a significant role in the human body’s defense against bacteria, viruses and parasites.
Analysis showed that the antibody binding site is relatively remote from the part of the virus that is responsible for preparation for penetration into human cells. Scientists also found that the binding region of an antibody is “hidden” in the virus and is only open to discovery at a certain point in time. The CR3022 antibody binds much less closely to SARS-CoV-2 and does not neutralize the coronavirus in laboratory tests.
Importantly, the findings suggest that the binding site of this antibody is a site prone to attacks, a antibodies that will bind more closely to it are likely to successfully neutralize the coronavirus. These antibodies can be used to treat COVID-19 patients and to provide temporary protection against the coronavirus to uninfected people. The researchers also point out that there may be antibodies that will effectively neutralize both SARS-CoV and SARS-CoV-2 as well as new coronaviruses that may potentially emerge.
Have a question about the coronavirus? Send them to the following address: [email protected]. You will find a daily updated list of answers HERE: Coronavirus – frequently asked questions and answers
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