It is indeed possible to enhance the antibodies that the body goes on to produce so as to fight SARS-CoV2. In a study conducted by Lund University researchers in Sweden, this was inferred by redesigning the antibodies as well as combining them against the virus. The modified antibodies have been tested across human cells as well as with mice.
Many antibodies that have been used for the treatment of the COVID infection during the pandemic have been referred to as neutralising antibodies that go on to prevent the virus from infecting the cells. But as the virus mutates, the ability of the antibodies to bind themselves to the virus is lost, and thus the protective effect as well.
In the present study, the researchers concentrated on the antibodies that can tag the virus that needs to be eliminated by the immune system’s immune cells, a process that’s called opsonization.
According to Pontus Nordenfelt, an associate professor and the researcher in infectious medicine who led the study, there often happens to be talk about wanting to neutralise viruses by preventing them from being bound to the body’s cells. Although it can work well, they would also like to trigger the ability of the immune system to eradicate the virus, which can be done by way of opsonizing antibodies that happen to mark the virus so that it can be eliminated.
It is well to note that the monoclonal antibodies come from a single clone and can be grown in the laboratory in cells for treatment as well as diagnostic purposes for various diseases. The researchers have made edits to eight opsonizing monoclonal antibodies in the current study by replacing the parts that signal the immune system to give a response. It was further investigated whether varied combinations of the antibodies could go on to improve their functions. Apparently, when the researchers switched the backbone of the Y-shaped antibody of one of the most common lgG antibodies in the blood, lgG1, towards the backbone of a theoretically more robust antibody, lgG3, a much stronger immune response was observed. These studies were carried out in human cells as well as mice.
As per the first author of the research, Arman Izadi, their preclinical trial inferences with human immune cells from the donors go on to suggest that the mix of these lgG3 antibodies could as well have a potent clinical effect against SARS-CoV-2 as well as its variants in cases where vaccines do not provide as much protection as they should.
The researchers designed monoclonal antibodies can also go ahead with binding to several sites on the same spike protein. This helps enhance the protection possibility, say researchers. The robust effect that can be seen with the cocktail can be gauged by the fact that there happen to be more antibodies across different places of the spike protein, which signals the immune cells and guides where the virus is. Significantly, the effect happened to be greatest with IgG3 cocktails and not with lgG1s. These go on to speak volumes about lgG3 and how promising it is for the treatment.
The researchers went on to have access to many antibodies, like SARS-CoV-2, of which eight happened to be of the lgG3 type. The next step in the research is to analyse whether these bind and protect against updated virus variants.
According to Pontus Norenfelt, the way of designing the antibodies to elevate their signalling ability opens novel possibilities to treat SARS-CoV-2 infections. They already have promising data, and should this work, an antibody can develop that provides protection against all the variants of SARS-CoV-2 as well as any future variants.