Indian researchers working towards developing effective vaccine strategies against SARS-CoV-2, HIV
Bengaluru: Indian Institute of Science claimed on Tuesday that researchers led by Raghavan Varadarajan, Professor at IISc's Molecular Biophysics Unit, are working towards developing effective vaccine strategies against two viruses: SARS-CoV-2 and HIV.
In two studies published in the past week, they reported the design of a 'heat-tolerant' COVID-19 vaccine candidate and a rapid method to identify specific regions on the HIV envelopeprotein that are targeted by antibodies, which can help design effective vaccines, an IISc press release said.
The studies were published in the Journal of Biological Chemistry and the Proceedings of the National Academy of Sciences respectively, according to Bengaluru-based IISc.
The COVID-19 vaccine candidate contains a part of the spike protein of the novel Coronavirus called the Receptor Binding Domain (RBD) - the region that helps the virus stick to the hosts cell.
It is being developed by Varadarajans lab in collaboration with Mynvax, a startup co-founded by him and incubated at IISc, as well as several other institutes.
"When tested in guinea pig models, the vaccine candidate triggered a strong immune response", the statement said.
"Surprisingly, it also remained stable for a month at 37C, and freeze-dried versions could tolerate temperatures as high as 100C.
Such 'warm' vaccines can be stored and transported without expensive cooling equipment to remote areas for mass vaccination - most vaccines need to be stored between 2-8C or even cooler temperatures to avoid losing their potency", it said.
Compared to newer types such as mRNA vaccines, making a protein-based vaccine like this can also be scaled up easily in India where manufacturers have been making similar vaccines for decades, IISc said.
There is another difference between the vaccine candidate being developed by Varadarajans team and many other COVID-19 vaccines in the works: it only uses a specific part of the RBD, a string of 200 amino acids, instead of the entire spike protein.
The team inserted genes coding for this part via a carrier DNA molecule called a plasmid, into mammalian cells, which then churned out copies of the RBD section.
They found that the RBD formulation was just as good as the full spike protein in triggering an immune response in guinea pigs, but much more stable at high temperatures for extended periods - the full spike protein quickly lost its activity at temperatures above 50C, according to the statement. "Now we have to get funds to take this forward to clinical development, says Varadarajan. This would include safety and toxicity studies in rats along with process development and GMP manufacture of a clinical trial batch, before they are tested in humans.