Immunoglobulin A1 protease activity in strains of Ureaplasma urealyticum.
Thirteen serovars of Ureaplasma urealyticum were analyzed for the ability to cleave human IgA. Strains of all of the serovars tested cleaved IgA 1 in the hinge region of the alpha-chain, resulting in intact Fc and monomeric Fab fragments. IgA 1 protease activity was also observed in concentrated cell-free extracts of spent cultivation medium, indicating that the IgA 1 protease was excreted into the medium during growth of the micro-organisms. Five clinical isolates of U. urealyticum obtained from urine, cervix, vagina, amniotic fluid, and synovial fluid were positive for IgA 1 protease activity. No proteolytic activity was observed against human IgA 2, IgG, or IgM. Strains of Mycoplasma fermentans, M. salivarium and seven serovars of M. hominis were negative for IgA 1 protease activity.
D007070:Immunoglobulin A / Q000378:metabolism; D010447:Peptide Hydrolases / Q000032:analysis*; D012697:Serine Endopeptidases; D014509:Ureaplasma / Q000201:enzymology*
D007070:Immunoglobulin A; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases; C021433:IgA-specific serine endopeptidase