Unveiling the structure, function and dynamics of StmPr1 in Stenotrophomonas maltophilia virulence.

ABSTRACT: The increase in infections caused by multi-resistant Gram-negative bacteria, like Stenotrophomonas maltophilia, has become a growing health crisis worldwide. S. maltophilia poses a risk because of its tendency to opportunistically infecting patience for example through colonization of catheters in hospital environments using its intrinsic resistance against multiple antibiotics. Through the COVID-19 pandemic it gained more prominence by being a key pathogen in respiratory co-infections. This study will present a structural analysis of StmPr1, S. maltophilia's main virulence factor, an excreted serine protease. Our study outline structure and functional aspects of StmPr1, revealing a unique autoproteolytic activity resulting in a shortened version of the active enzyme. We also investigated

SUBMITTER: Sommer M 

PROVIDER: S-EPMC12181431 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature