Antibodies are a hot topic in COVID-19 research | Instant News

Researchers at the Hutch led by bloom developed a pilot study allows researchers who do not have access to a high level of Biosafety in the laboratories in order to safely measure neutralizing antibodies to SARS-cov-2. The test measures how well antibodies against a harmless virus that has been genetically engineered to carry SARS-cov-2 spikes, so it simulates a real virus. This “pseudovirus” can be used to test COVID-19 vaccine or therapy of the antibodies in the laboratory without the use of dangerous wild viruses, which can be verified only in highly secure facilities.

This test was decisive for the other Hutch team, led by immunologist Dr. Leo Stamatatosin his research of antibodies that specifically bind with a characteristic burst on the surface of the coronavirus, a likely target for vaccines and therapies.

In journal of immunity, Stamatatos and colleagues describe how they have identified from the blood COVID-19 survivors of extremely potent neutralizing antibodies that could block the virus ‘ ability to block vulnerable cells considered their main goal inside the human lung.

The antibody fits so tightly to a spot on the top of SARS-cov-2 spike that he stopped the infection 100% of the time using laboratory tests bloom.

“Because it neutralized all of the viral particles in our analysis, this theory is a good candidate for COVID-19 therapy or vaccine,” said Stamatatos.

His team started with Washington state University researchers in the beginning of March in an effort to identify the natural protective antibodies against SARS-coronavirus-2 shortly after receiving a valuable blood sample from a patient who recovered from COVID-19.

They have developed a test to isolate antibodies that is one patient, of course, is created against coronavirus and identified 45 different varieties that have locks on one site or another uneven surface protein spike. Of these, only three had no way to block the infection.

Main performer

One antibody that seemed to hit the bulls-eye was measured 530 times more powerful than its closest competitors: the other two, which are placed in different parts of the spike of coronaviruses, but only weakly blocked the infection.

Top-performer, with the inscription CV30, was extremely effective to stop infection, probably because it was locked securely, so that the edge at the tip of the tongue is called the binding domain of the receptor. That is the same site that was so problematic for a person because it connects nodes that spike is like a key in a lock, a receptor called ACE2 and found on the surface of cells that line the deepest recesses of human lungs.

ACE2 and acts as a trap door allows the coronavirus to break into these cells and use their internal genetic mechanisms to make thousands of new copies of SARS-cov-2, eventually killing the cells.

Can this antibody, by itself, to be the key to stopping the pandemic? Stamatatos said probably not, because the virus eventually escape through mutations that closely matched the site on its edge. Thus, the researchers hope to develop a cocktail of different neutralizing antibodies.

“Ideally, the cocktail seems that might be better because the virus has less chance to survive,” said study co-author Dr. Andrew McGuirethe laboratory which performed the genetic sequencing of antibodies and conducted a study of neutralization using pseudovirus test bloom.

Stamatatos and his colleagues are now studying whether neutralizing antibodies isolated using these methods can be formulated in infusion, which could protect those who are directly involved with the infection, or as a treatment to limit viral replication in already infected patients.

The structure of the successful antibodies can also inform research on the development of a vaccine that will be designed to teach the immune system of a healthy person for such protective proteins when exposed to SARS-cov-2, inhibiting the infection.

Meanwhile, McGuire is working on neutralizing antibodies against coronaviruses within a few years, in collaboration with biochemist Dr. David Veesler at the University of Washington. To COVID-19, the work was initially intended to SARS and MERS, two deadly epidemics — discovered in 2003 and 2012, respectively — caused by a coronavirus cousin of SARS-cov-2.

That gave researchers an impetus describing the structure of the SARS-cov-2 spike and Veesler and Maguire were co-authors one of the first documents to describe it.

The team hopes to identify an antibody that neutralizes all three forms of the deadly coronavirus, which can be converted in the antibody therapeutic for the treatment of infection with any of these threats coronavirus.


image source

to request modification Contact us at Here or [email protected]