An interesting immunotherapeutic approach

IBBR collaborates with Integrated BioTherapeutics to advance a novel approach to treating infectious disease

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ROCKVILLE, Md.—Institute for Bioscience and Biotechnology Research (IBBR) Fellow Dr. Daniel Nelson, associate professor, department of Veterinary Medicine, University of Maryland, College Park, is working on an innovative approach to treating bacterial disease in collaboration with Dr. Rajan Adhikari, assistant director of Bacteriology at Integrated BioTherapeutics (IBT), and George Mason University’s Dr. Ramin Hakami, associate professor, School of Systems Biology and National Center for Biodefense and Infectious Diseases.
The group recently received a $3 million Phase 2 STTR award from the National Institutes of Health that will fund advancement of their novel immunotherapeutic into non-human primates, as well as optimization of a cell line for biomanufacturing the drug. This work is supported by NIH awards to IBT. The awards are part of the federal Small Business Technology Transfer (STTR) program, which aims to facilitate cooperation between small businesses and US research institutions to bridge the gap between basic research and commercialization.
Most people are familiar with taking antibiotics to treat bacterial infections, and know that some infections can be prevented with vaccines. Vaccines cause the body to make antibodies. Researchers are also engineering antibodies to use as immunotherapeutic drugs.
All of these approaches attack the pathogens, but some bacteria release toxins with dangerous capabilities to cause damage far from the site of infection. Since patients can still be in danger even after the bacteria are killed, the current treatment for such toxemias is two-pronged: antibiotics to kill the bacteria and antibodies to neutralize the toxin. But what if one therapeutic could do both?   
Nelson and his collaborators have engineered and preclinically tested a single immunotherapeutic composed of a humanized antibody that binds toxin, and a protein that binds tightly to the bacterial surface. Together these components specifically direct the antibodies to the site of the infection, where they neutralize toxin and signal the immune system to kill the bacteria. The surface-binding component is derived from a bacteriophage endolysin protein characterized in Nelson’s laboratory.
“This Phase 2 award is an important step toward translating Dr. Nelson’s academic endolysin research from the lab to the market,” notes IBBR director Dr. Thomas Fuerst. “The advancement of this technology moves us closer to providing a more efficient and effective treatment for bacterial infections.”

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