Scientists have designed new antibodies that can effectively protect the Ebola virus.
A study, published in the Cell Reports, showed that DNA-encoded monoclonal antibodies (DMAbs) were expressed over a long period of time and offered complete and long-term protection against the deadly challenges of the virus.
According to the Wistar Institute scientists in the US, DMAbs can also provide a new powerful platform for the rapid screening of monoclonal antibodies that enhance preclinical growth.
Ebola infection causes a catastrophic disease, known as Ebola virus, for which no authorized vaccine or treatment is available. The epidemic of Zaire Ebola virus for the period 2014-2016 in West Africa was the most serious that has been reported so far, with more than 28,600 cases and 11,325 deaths according to the US Disease Control Center.
A new outbreak has begun in the Democratic Republic of Congo, with more than 200 people since August.
One of the experimental pathways pursued by scientists is to evaluate the safety and efficacy of monoclonal antibodies isolated from survivors as promising candidates for further development as therapeutic agents against Ebola virus infection.
However, this approach requires high doses and repeated administration of recombinant monoclonal antibodies that are complex and expensive to manufacture, so that meeting global demand, while maintaining cost at affordable prices, is difficult.
"Our studies show the development of a new platform that quickly combines aspects of monoclonal antibody detection technology and development technology with the revolutionary properties of synthetic DNA technology," said David B Weiner, of the Wistar Institute.
The team designed and improved optimized DMAbs, which, when injected locally, provides the body's genetic design to make functional and protective Ebola-specific antibodies, bypassing the multiple stages in the antibody growth and production process.
Dozens of DMAbs were tested in mice and the best selected were selected for further studies. These have proved to be particularly effective in providing full protection against disease in challenge studies.
"Due to the inherent biochemical properties, some monoclonal antibodies may be difficult and grow slowly or even impossible to construct, fall out of the developmental process and cause loss of potentially effective molecules," Weiner said.
"The DMAb platform allows us to collect protective antibodies from protected individuals and engineers and compare them quickly and then deliver them in vivo to protect against infectious challenges," he said.
"Such an approach could be important during an epidemic when we need to design, evaluate and deliver salvage therapies in the right way," he added.
(This story has not been edited by Business Standard staff and is automatically generated by syndication.)