Limited proteolysis of neutrophil granule proteins by the bacterial protease RgpB depletes neutrophil antimicrobial capacity.

ABSTRACT: Neutrophils are highly abundant in the gingival tissues where they play an essential role in immune homeostasis by preventing microbial invasion. Here, we show that the oral periodontal pathogen Porphyromonas gingivalis utilizes its cysteine proteases (gingipains) to disengage phagosomal antimicrobial capacity. Arginine gingipains are a subfamily of trypsin-like proteases produced by P. gingivalis that cleave several host proteins at arginine residues. We find that RgpB-mediated proteolysis of host proteins is not limited to the extracellular or plasma membrane-associated host proteins, but also results in the degradation of several intracellular proteins. Using 2D-difference gel electrophoresis coupled with mass spectrometry, we identified several cytoskeletal and cytoplasmic proteins, in

SUBMITTER: Cooper KN 

PROVIDER: S-EPMC11878996 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature