Arginine-specific gingipain (Rgp)

Arginine-specific gingipain is a bacterial cysteine protease produced by *Porphyromonas gingivalis*, a major pathogen in chronic periodontitis and implicated in systemic diseases such as Alzheimer's disease. The enzyme exists primarily in two forms, RgpA and RgpB, distinguished by minor differences in substrate specificity and domain structure. Rgps cleave peptide bonds after arginine residues, playing a critical role in tissue invasion, immune evasion, and disruption of host inflammatory responses by degrading proteins such as extracellular matrix components, SLPI, cytokines, and cell adhesion molecules[1][4][5]. These activities facilitate nutrient acquisition for the bacterium and contribute to both local and systemic disease processes. Ongoing research explores selective inhibition of Rgps as a therapeutic approach for preventing or treating periodontitis and modifying downstream risks such as neurodegeneration[2][5].

Other names

RgpARgpBarginine gingipainarginine-specific cysteine proteasegingipain R

Cleavage of peptide bonds following arginine residues in host proteins; Proteolytic inactivation of host defense proteins (e.g., secretory leukocyte protease inhibitor, SLPI); Degradation of extracellular matrix, cytokines, and cell adhesion molecules