Glutamyl endopeptidase (Staphylococcus aureus) (V8 protease)

Glutamyl endopeptidase, commonly known as Staphylococcus aureus V8 protease (SspA), is a major extracellular serine protease secreted by the pathogen S. aureus [1]. The enzyme is highly specific, cleaving peptide bonds at the carboxyl side of glutamic acid and, under certain conditions, aspartic acid residues [2]. SspA serves as a critical virulence factor by degrading a wide array of host proteins, including immunoglobulins, fibrinogen, and antimicrobial peptides, which facilitates bacterial invasion and helps the pathogen evade the host immune response [3]. In clinical contexts, V8 protease is strongly associated with the pathogenesis of atopic dermatitis, where it contributes to the degradation of the epidermal barrier and promotes chronic inflammation [4]. While there are currently no FDA-approved drugs specifically targeting V8 protease, it is a significant subject of research for anti-virulence therapies that aim to reduce bacterial pathogenicity without inducing the selective pressure associated with traditional antibiotics [5]. [1] UniProt (P0C0Q4); [2] MEROPS Database (S51.001); [3] PMID: 15576779; [4] PMID: 25104302; [5] PMID: 30254018.

Other names

Endoproteinase Glu-CStaphylococcal serine proteaseSspAV8 enzymeProtease V8

Cleavage of peptide bonds C-terminal to glutamic acid and aspartic acid residues via a serine protease catalytic triad mechanism, which can be inhibited by serine protease inhibitors to prevent host tissue damage.