Integral Molecular News

Integral Molecular Awarded $9.1 Million Contract from NIAID to Map Epitopes on Viral Pathogens using Shotgun Mutagenesis Mapping Technology

PHILADELPHIA–(BUSINESS WIRE)–Integral Molecular, Inc. has been selected to receive a five year, $9.1 million contract from the National Institute of Allergy and Infectious Disease (NIAID), part of the National Institutes of Health, to elucidate novel B cell epitopes on the surface of viral pathogens. Integral Molecular’s Shotgun Mutagenesis Mapping technology will be used to identify both linear and conformational epitopes on viral envelope proteins. By helping to define the full range of immunodominant structures on viral pathogens, Shotgun Mutagenesis will facilitate the design and development of improved vaccines against emerging infectious diseases. This is the second NIH award recently received by Integral Molecular for epitope mapping services.

“Understanding the full range of viral epitopes targeted by the human immune system is vital to designing better viral vaccines,” said Dr. Benjamin Doranz, President of Integral Molecular. “This project will result in hundreds of new human antibodies against important viral proteins, high resolution epitope maps describing how these antibodies bind to their targets, and structural information about how these viral proteins function.”

“We are extremely excited to have generated inhibitory MAbs that target P2X3. This is an exciting advancement for the chronic pain field where there are limited therapeutic options,” said Joseph Rucker, Director of Research and Development at Integral Molecular. “Because of their structural complexity and conservation, ion channels have been exceptionally challenging to target and inhibit and these P2X3 MAbs represent some of the few inhibitory antibodies against any ion channel. We are eager to move this campaign forward and progress our most promising leads into development to treat neuropathic pain”.

Shotgun Mutagenesis Mapping analyzes hundreds to thousands of variants of a target protein, each variant containing a unique amino acid substitution, to rapidly identify the binding residues that form antibody epitopes. This technology is well suited for epitope mapping viral envelope proteins, which usually form complex oligomeric structures and contain post-translational modifications that require expression within mammalian cells to retain their native conformation. Because Shotgun Mutagenesis maps functional proteins directly within living human cells, target proteins do not require purification or extraction from their native environment.

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