Streptococcus suis IgM protease and related Streptococcus suis antigens

Streptococcus suis IgM protease, primarily known as IdeSsuis, is a 124 kDa cysteine protease secreted by the porcine pathogen Streptococcus suis (Seele et al., 2013). Its primary biological function is the highly specific cleavage of porcine IgM between the C2 and C3 domains, which disrupts the classical complement pathway and allows the bacteria to evade the host's early immune response (Seele et al., 2015). This target also encompasses related Streptococcus suis antigens, such as suilysin (Sly), muramidase-released protein (MRP), and surface antigen one (Sao), which are frequently combined in vaccine formulations to enhance protective efficacy (Patent US11607447). These antigens are critical for the development of recombinant subunit vaccines aimed at preventing invasive diseases like meningitis, septicemia, and arthritis in swine. By inducing the production of opsonizing antibodies, these vaccines restore the host's ability to clear the pathogen and reduce the risk of zoonotic transmission to humans. The targeting of these proteins represents a key strategy for improving animal health and reducing antibiotic use in the global swine industry.

Other names

IdeSsuisIgM-degrading enzyme of Streptococcus suisS. suis vaccine antigensStreptococcus suis virulence factorsIgM protease of S. suis

Induction of neutralizing and opsonizing antibodies that inhibit the enzymatic activity of the IgM protease and other virulence factors, thereby preventing immune evasion and facilitating bacterial clearance by host phagocytes.