IdeE, an IgG-endopeptidase of Streptococcus equi ssp. equi.
Abstract: Streptococcus equi ssp. equi is the causative agent of strangles, a highly contagious and serious disease in the upper respiratory tract of horses. The present study describes the characterization of IdeE, a homolog of the secreted IgG-specific protease IdeS/Mac of Streptococcus pyogenes. The activity of IdeE is compared with the activity of IdeZ, the corresponding enzyme of the closely related S. equi ssp. zooepidemicus. A study of the proteolytic activity of recombinant IdeE and IdeZ on IgG from a selection of mammals shows that only antibodies containing the substrate site of IdeS/Mac are cleaved, indicating that the specificities of these enzymes are similar. Interestingly, IgG from horse is less effectively cleaved than IgG from e.g. dog or humans, as the dominating IgG isotype in horse sera (IgG4) lacks a distinct substrate site for IdeE/IdeZ. IgG-degradation is observed when S. equi ssp. equi is grown in the presence of horse serum, but not when grown with purified IgG. As the fraction of degraded IgG contains IgG4, the observed activity might be due to the expression of an unknown enzyme rather than IdeE. In a similar assay, no proteolysis of IgG was detected in the growth media of S. equi ssp. zooepidemicus.
Publication Date: 2006-08-23 PubMed ID: 16923080DOI: 10.1111/j.1574-6968.2006.00404.xGoogle Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This research article is primarily about the study and comparison of enzymes IdeE and IdeZ from Streptococcus equi, bacteria responsible for strangles in horses, and their action on differing antibodies from various animals, with notable findings on their behavior in horse serum.
Introduction and Aim
- The primordial aim of the study is to scrutinize the proteolytic (protein-breaking) activity of enzymes IdeE and IdeZ, present in different strains of Streptococcus equi.
- Streptococcus equi is a bacterium, particularly harmful to horses, causing a severe respiratory disease known as strangles.
Characterization of IdeE and IdeZ
- IdeE and IdeZ are homologous to another protease (a type of enzyme that catalyses the breaking of peptide bonds) called IdeS/Mac, present in Streptococcus pyogenes.
- The research involved assessing the action of these enzymes on Immunoglobulin G (IgG), a type of antibody prevalent in mammals.
Comparative Study of IdeE and IdeZ
- The study compares the activity of IdeE and IdeZ enzymes on IgG from a variety of mammals.
- The findings suggest that these enzymes only cleave antibodies that contain the substrate (a molecule on which an enzyme acts) site of IdeS/Mac.
- This shows that IdeE and IdeZ have similar specificities or behaviors in their enzymatic activity to IdeS/Mac.
Findings on IdeE and IdeZ Activity in Horse Sera
- The study found that IgG from horses is not as efficiently cleaved or broken down by these enzymes compared to IgG from dogs or humans.
- It was noted in particular that the most abundant type of IgG in horse serum, IgG4, lacks a distinct substrate site for IdeE/IdeZ, explaining the reduced cleavage.
Observations on IdeE and IdeZ Activity in Growth Media
- The research observed that S. equi ssp. equi, grown in the presence of horse serum showed degradation of IgG, unlike when grown with purified IgG. This suggests that the observed activity might not result from IdeE, but rather from the expression of an unknown enzyme.
- In a parallel experiment, no proteolysis of IgG was detected in the growth media of S. equi ssp. zooepidemicus.
Cite This Article
APA
Lannergård J, Guss B.
(2006).
IdeE, an IgG-endopeptidase of Streptococcus equi ssp. equi.
FEMS Microbiol Lett, 262(2), 230-235.
https://doi.org/10.1111/j.1574-6968.2006.00404.x Publication
Researcher Affiliations
- Department of Microbiology, Swedish University of Agricultural Sciences, Uppsala, Sweden. jonas.lannergard@mikrob.slu.se
MeSH Terms
- Animals
- Bacterial Proteins / genetics
- Bacterial Proteins / metabolism
- Blotting, Western
- Electrophoresis, Polyacrylamide Gel
- Genes, Bacterial
- Horses / immunology
- Immunoglobulin G / metabolism
- Mammals / immunology
- Mass Spectrometry
- Polymerase Chain Reaction
- Recombinant Proteins / genetics
- Recombinant Proteins / metabolism
- Serum
- Streptococcus equi / genetics
- Streptococcus equi / metabolism
- Substrate Specificity
Citations
This article has been cited 19 times.- Breitfelder AK, Schrödl W, Rungelrath V, Baums CG, Alber G, Schütze N, Müller U. Immunoglobulin M-degrading enzyme of Streptococcus suis (Ide (Ssuis) ) impairs porcine B cell signaling.. Front Immunol 2023;14:1122808.
- Ros-Gañán I, Hommel M, Trigueros-Motos L, Tamarit B, Rodríguez-García E, Salas D, Pérez G, Douar A, Combal JP, Benichou B, Ferrer V, González-Aseguinolaza G. Optimising the IgG-degrading enzyme treatment regimen for enhanced adeno-associated virus transduction in the presence of neutralising antibodies.. Clin Transl Immunology 2022;11(2):e1375.
- Frosth S, Morris ERA, Wilson H, Frykberg L, Jacobsson K, Parkhill J, Flock JI, Wood T, Guss B, Aanensen DM, Boyle AG, Riihimäki M, Cohen ND, Waller AS. Conservation of vaccine antigen sequences encoded by sequenced strains of Streptococcus equi subsp. equi.. Equine Vet J 2023 Jan;55(1):92-101.
- Habazin S, Štambuk J, Šimunović J, Keser T, Razdorov G, Novokmet M. Mass Spectrometry-Based Methods for Immunoglobulin G N-Glycosylation Analysis.. Exp Suppl 2021;112:73-135.
- Bai Q, Ma J, Zhang Z, Zhong X, Pan Z, Zhu Y, Zhang Y, Wu Z, Liu G, Yao H. YSIRK-G/S-directed translocation is required for Streptococcus suis to deliver diverse cell wall anchoring effectors contributing to bacterial pathogenicity.. Virulence 2020 Dec;11(1):1539-1556.
- Machacek M, Fields PE, Slawson C. A proteolytic method for evaluating O-GlcNAcylation on proteins of similar molecular weight to antibody heavy chain after immunoprecipitation.. Anal Biochem 2020 Dec 15;611:114001.
- Cohen ND, Cywes-Bentley C, Kahn SM, Bordin AI, Bray JM, Wehmeyer SG, Pier GB. Vaccination of yearling horses against poly-N-acetyl glucosamine fails to protect against infection with Streptococcus equi subspecies equi.. PLoS One 2020;15(10):e0240479.
- Elmore ZC, Oh DK, Simon KE, Fanous MM, Asokan A. Rescuing AAV gene transfer from neutralizing antibodies with an IgG-degrading enzyme.. JCI Insight 2020 Sep 17;5(19).
- Xiao G, Wu Z, Zhang S, Tang H, Wang F, Lu C. Mac Protein is not an Essential Virulence Factor for the Virulent Reference Strain Streptococcus suis P1/7.. Curr Microbiol 2017 Jan;74(1):90-96.
- Spoerry C, Hessle P, Lewis MJ, Paton L, Woof JM, von Pawel-Rammingen U. Novel IgG-Degrading Enzymes of the IgdE Protease Family Link Substrate Specificity to Host Tropism of Streptococcus Species.. PLoS One 2016;11(10):e0164809.
- Seele J, Singpiel A, Spoerry C, von Pawel-Rammingen U, Valentin-Weigand P, Baums CG. Identification of a novel host-specific IgM protease in Streptococcus suis.. J Bacteriol 2013 Mar;195(5):930-40.
- Flock M, Frykberg L, Sköld M, Guss B, Flock JI. Antiphagocytic function of an IgG glycosyl hydrolase from Streptococcus equi subsp. equi and its use as a vaccine component.. Infect Immun 2012 Aug;80(8):2914-9.
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- Ishihara K, Wawrzonek K, Shaw LN, Inagaki S, Miyamoto M, Potempa J. Dentipain, a Streptococcus pyogenes IdeS protease homolog, is a novel virulence factor of Treponema denticola.. Biol Chem 2010 Sep;391(9):1047-55.
- Liu M, Lei B. IgG Endopeptidase SeMac does not Inhibit Opsonophagocytosis of Streptococcus equi Subspecies equi by Horse Polymorphonuclear Leukocytes.. Open Microbiol J 2010 Apr 8;4:20-5.
- Guss B, Flock M, Frykberg L, Waller AS, Robinson C, Smith KC, Flock JI. Getting to grips with strangles: an effective multi-component recombinant vaccine for the protection of horses from Streptococcus equi infection.. PLoS Pathog 2009 Sep;5(9):e1000584.
- Holden MT, Hauser H, Sanders M, Ngo TH, Cherevach I, Cronin A, Goodhead I, Mungall K, Quail MA, Price C, Rabbinowitsch E, Sharp S, Croucher NJ, Chieu TB, Mai NT, Diep TS, Chinh NT, Kehoe M, Leigh JA, Ward PN, Dowson CG, Whatmore AM, Chanter N, Iversen P, Gottschalk M, Slater JD, Smith HE, Spratt BG, Xu J, Ye C, Bentley S, Barrell BG, Schultsz C, Maskell DJ, Parkhill J. Rapid evolution of virulence and drug resistance in the emerging zoonotic pathogen Streptococcus suis.. PLoS One 2009 Jul 15;4(7):e6072.
- Söderberg JJ, Engström P, von Pawel-Rammingen U. The intrinsic immunoglobulin g endopeptidase activity of streptococcal Mac-2 proteins implies a unique role for the enzymatically impaired Mac-2 protein of M28 serotype strains.. Infect Immun 2008 May;76(5):2183-8.
- Hess JL, Porsch EA, Shertz CA, Boyle MD. Immunoglobulin cleavage by the streptococcal cysteine protease IdeS can be detected using protein G capture and mass spectrometry.. J Microbiol Methods 2007 Aug;70(2):284-91.
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