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Armata Pharmaceuticals Announces Structural Biology Publication

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Publication describes the structure of phage Pa193, a top candidate for inclusion into Armata's multi-phage anti-Pseudomonas clinical products

LOS ANGELES, Oct. 30, 2024 /PRNewswire/ -- Armata Pharmaceuticals, Inc. (NYSE American: ARMP) ("Armata" or the "Company"), a biotechnology company focused on the development of high-purity, pathogen-specific bacteriophage therapeutics for antibiotic-resistant and difficult-to-treat bacterial infections, today announced a paper in Communications Biology, published by Nature Portfolio.

Armata Pharmaceuticals Logo (PRNewsfoto/Armata Pharmaceuticals, Inc.)
Armata Pharmaceuticals Logo (PRNewsfoto/Armata Pharmaceuticals, Inc.)

The publication, titled, "Cryo-EM analysis of Pseudomonas phage Pa193 structural components," describes the structure of phage Pa193. Pa193 is representative of a family of phages present in Armata's multi-phage clinical candidate, AP-PA02, which the company is developing to treat chronic Pseudomonas aeruginosa infections in patients with cystic fibrosis (CF) or non-cystic fibrosis bronchiectasis (NCFB).

"We are very pleased to simultaneously advance the fundamental understanding of phage structure while remaining laser focused on phage function in full clinical development. One of our phage clinical candidates contributed to the important learnings from this study," stated Dr. Deborah Birx, Chief Executive Officer of Armata. "As we continue to advance our proprietary development programs, which are founded on uncompromising science and rigorously designed clinical trials, this study furthers our understanding of phage structural components and how changes in phage biology may expand their clinical utility to other dangerous pathogens beyond P. aeruginosa, potentially informing future development plans."

Dr. Gino Cingolani, Anderson Family Endowed Chair in Medical Education, Research & Patient Care and Professor in the Department of Biochemistry and Molecular Genetics, The University of Alabama at Birmingham, and co-author of the paper, stated, "This research highlights our ability to decipher a whole virus at the single atom resolution. Leveraging cryogenic electron microscopy, proteomics and bioinformatic analysis, we are now able to take a complete inventory of all structural components of a large macromolecular assembly, such as Pa193. The opportunities are endless. From a basic-science standpoint, understanding both the architecture and design principles of Pa193 provides valuable insight into its stability and mechanisms of genome-delivery. These findings can be generalized to other members of the Pa193 phage family and aid in structure prediction and protein engineering, valuable to using phages as biomedicines for therapeutic applications."