title: Identification and Characterization of IgdE, a Novel IgG-degrading Protease of Streptococcus suis with Unique Specificity for Porcine IgG.
abstract: Streptococcus suisis a major endemic pathogen of pigs causing meningitis, arthritis, and other diseases. ZoonoticS. suisinfections are emerging in humans causing similar pathologies as well as severe conditions such as toxic shock-like syndrome. Recently, we discovered an IdeS family protease ofS. suisthat exclusively cleaves porcine IgM and represents the first virulence factor described, linkingS. suisto pigs as their natural host. Here we report the identification and characterization of a novel, unrelated protease ofS. suisthat exclusively targets porcine IgG. This enzyme, designated IgdE forimmunoglobulinG-degradingenzyme ofS. suis, is a cysteine protease distinct from previous characterized streptococcal immunoglobulin degrading proteases of the IdeS family and mediates efficient cleavage of the hinge region of porcine IgG with a high degree of specificity. The findings that allS. suisstrains investigated possess the IgG proteolytic activity and that piglet serum samples contain specific antibodies against IgdE strongly indicate that the protease is expressedin vivoduring infection and represents a novel and putative important bacterial virulence/colonization determinant, and a thus potential therapeutic target.
authors: From the Department of Molecular Biology and Umeå Centre for Microbial Research, Umeå University, 90187 Umeå, Sweden.
authors: Christian
authors: C
authors: Spoerry
authors: the Institute for Microbiology, Center for Infection Medicine, University of Veterinary Medicine Hannover, 30173 Hannover, Germany, and.
authors: Jana
authors: J
authors: Seele
authors: the Institute for Microbiology, Center for Infection Medicine, University of Veterinary Medicine Hannover, 30173 Hannover, Germany, and.
authors: Peter
authors: P
authors: Valentin-Weigand
authors: the Institute for Microbiology, Center for Infection Medicine, University of Veterinary Medicine Hannover, 30173 Hannover, Germany, and the Institute for Bacteriology und Mycology, Centre for Infectious Diseases, College of Veterinary Medicine, University Leipzig, 04103 Leipzig, Germany.
authors: Christoph G
authors: CG
authors: Baums
authors: From the Department of Molecular Biology and Umeå Centre for Microbial Research, Umeå University, 90187 Umeå, Sweden, ulrich.von-pawel@molbiol.umu.se.
authors: Ulrich
authors: U
authors: von Pawel-Rammingen
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D020134:Catalytic Domain; D057056:Cysteine Proteases / Q000737:chemistry / Q000378:metabolism*; D007074:Immunoglobulin G / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D059748:Proteolysis; D013290:Streptococcal Infections / Q000378:metabolism / Q000662:veterinary*; D017011:Streptococcus suis / Q000201:enzymology* / Q000378:metabolism; D013379:Substrate Specificity; D013552:Swine / Q000378:metabolism / Q000382:microbiology*
chemical_list: D001426:Bacterial Proteins; D007074:Immunoglobulin G; D057056:Cysteine Proteases
keywords: Streptococcus; antibody; cysteine protease; immunoglobulin G (IgG); proteolytic enzyme; substrate specificity