Immunoglobulin M-degrading enzyme of Streptococcus suis (Ide Ssuis ) impairs porcine B cell signaling

( ) is an important porcine pathogen, causing severe disease like meningitis and septicemia primarily in piglets. Previous work showed that the IgM-degrading enzyme of (Ide ) specifically cleaves soluble porcine IgM and is involved in complement evasion. The objective of this study was to investigate Ide cleavage of the IgM B cell receptor and subsequent changes in B cell receptor mediated signaling. Flow cytometry analysis revealed cleavage of the IgM B cell receptor by recombinant (r) Ide _homologue as well as Ide derived from culture supernatants of serotype 2 on porcine PBMCs and mandibular lymph node cells. Point-mutated rIde _homologue_C195S did not cleave the IgM B cell receptor. After receptor cleavage by rIde _homologue, it took at least 20 h for mandibular lymph node cells to restore the IgM B cell receptor to levels comparable to cells previously treated with rIde _homologue_C195S. B cell receptor mediated signaling after specific stimulation the F(ab') portion was significantly inhibited by rIde _homologue receptor cleavage in IgM B cells, but not in IgG B cells. Within IgM cells, CD21 B2 cells and CD21 B1-like cells were equally impaired in their signaling capacity upon rIde _homologue B cell receptor cleavage. In comparison, intracellular B cell receptor independent stimulation with tyrosine phosphatase inhibitor pervanadate increased signaling in all investigated B cell types. In conclusion, this study demonstrates Ide cleavage efficacy on the IgM B cell receptor and its consequences for B cell signaling.