Los Angeles – September 08, 2026 -- Armata Pharmaceuticals, Inc. (NYSE American: ARMP) said a peer-reviewed paper in the Journal of Molecular Biology has mapped near-atomic resolution structures of eleven proteins in its Ar-KM bacteriophage, a Pseudomonas aeruginosa-targeting phage tied to the company's late-stage AP-PA02 program.
Researchers built atomic models of eleven structural proteins using cryo-electron microscopy
The study, titled "Insights into Genome Ejection by a Therapeutic phiKMV-like Bacteriophage," combined cryo-electron microscopy, proteomics and bioinformatics to capture three distinct states of the Ar-KM phage particle from a single purified preparation. The paper is published as J Mol Biol. 2026 Nov 1; 438(21):169993. AP-PA02, an inhaled bacteriophage candidate, has completed Phase 2 studies in cystic fibrosis and non-CF bronchiectasis patients with chronic pulmonary P. aeruginosa infection.
Study identifies enzyme activity and a new protein enabling genome delivery into bacteria
The research team found that Ar-KM securely packages its genetic material before infection and identified an enzyme activity that helps the phage penetrate the bacterial cell envelope. Investigators also characterized a previously unrecognized protein that coordinates release and delivery of the phage genome into P. aeruginosa.
Armata CEO Deborah Birx calls the findings the fourth publication from a UAB collaboration
"Stability before infection and efficient genome delivery at the point of infection are fundamental characteristics of a viable phage therapeutic, and this work provides important new insight into how Ar-KM can achieve both," said Dr. Deborah Birx, Chief Executive Officer of Armata and a co-author of the paper. Birx noted the collaboration with Dr. Gino Cingolani's group at the University of Alabama at Birmingham has now produced four publications, all characterizing the company's Pseudomonas aeruginosa phages.
Armata extends structural analysis to its Staphylococcus aureus phage candidates
Dr. Gino Cingolani, senior author of the paper and Anderson Family Endowed Chair in Medical Education, Research & Patient Care at UAB, said the work characterized Ar-KM at near-atomic resolution using cryo-electron microscopy, comparative genomics and mass spectrometry. Armata said it is now applying cryo-EM reconstruction to its proprietary Staphylococcus aureus phages, supported by proprietary purification processes the company credits for enabling the high-quality phage preparations required for high-resolution structural analysis.