A secreted 35 kDa protein, does not require processing or activation to exert its enzymatic activity. Also described as a CD11b homolog protein, Mac, CD11b is the α chain of complement receptor 3 (CR3), which is the receptor on phagocytes that recognizes C3b. ...
A secreted 35 kDa protein, does not require processing or activation to exert its enzymatic activity. Also described as a CD11b homolog protein, Mac, CD11b is the α chain of complement receptor 3 (CR3), which is the receptor on phagocytes that recognizes C3b. ...
Two more zinc metalloproteinase ZmpB and ZmpC may also contribute to virulence. Cleaves the Pro227-Thr228 peptide bond in the IgA1 hinge. May enable pathogens to subvert the antigen specificity of the humoral immune response to facilitate adhesive interactions and persistence on the mucosal surface. ...
Two more zinc metalloproteinase ZmpB and ZmpC may also contribute to virulence. Cleaves the Pro227-Thr228 peptide bond in the IgA1 hinge. May enable pathogens to subvert the antigen specificity of the humoral immune response to facilitate adhesive interactions and persistence on the mucosal surface. ...
Two more zinc metalloproteinase ZmpB and ZmpC may also contribute to virulence. Cleaves the Pro227-Thr228 peptide bond in the IgA1 hinge. May enable pathogens to subvert the antigen specificity of the humoral immune response to facilitate adhesive interactions and persistence on the mucosal surface. ...
Two more zinc metalloproteinase ZmpB and ZmpC may also contribute to virulence. Cleaves the Pro227-Thr228 peptide bond in the IgA1 hinge. May enable pathogens to subvert the antigen specificity of the humoral immune response to facilitate adhesive interactions and persistence on the mucosal surface. ...
Two more zinc metalloproteinase ZmpB and ZmpC may also contribute to virulence. Cleaves the Pro227-Thr228 peptide bond in the IgA1 hinge. May enable pathogens to subvert the antigen specificity of the humoral immune response to facilitate adhesive interactions and persistence on the mucosal surface. ...