Two novel IgG endopeptidases of Streptococcus equi.
Abstract: Streptococcus equi ssp. equi causes strangles, a highly contagious and serious disease in the upper respiratory tract of horses. Streptococcus equi ssp. zooepidemicus, another subspecies of this genus, is regarded as an opportunistic commensal in horses. The present study describes the characterization of two novel immunoglobulin G (IgG) endopeptidases of these subspecies, IdeE2 and IdeZ2. Both enzymes display sequence similarities with two previously characterized IgG endopeptidases, IdeE of S. equi ssp. equi and IdeZ of S. equi ssp. zooepidemicus. IdeE2 and IdeZ2 display high substrate-specificity in comparison with IdeE and IdeZ, as they both completely cleave horse IgG, while the activity against IgG from mouse, rabbit, cat, cow, sheep and goat is low or absent. The potential use of IdeE and IdeE2 as vaccine components was studied in a mouse infection model. In this vaccination and challenge study, both enzymes induced protection against S. equi ssp. equi infection.
Publication Date: 2009-08-08 PubMed ID: 19659725DOI: 10.1111/j.1574-6968.2009.01698.xGoogle Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This research article discusses a study on two new types of proteins found in two subspecies of bacteria known to affect horses’ respiratory tracts. These proteins are found to be highly specific for horse antibodies and may be useful in the development of vaccines.
Details on the Studied Pathogens
- The research focuses on two pathogens: Streptococcus equi ssp. equi and Streptococcus equi ssp. zooepidemicus which are both known to affect the upper respiratory tracts of horses.
- The former is responsible for causing a highly contagious disease known as strangles, while the latter is considered as an opportunistic commensal, meaning it lives harmlessly inside horses under normal circumstances but can cause illness under specific conditions.
Introduction of Novel IgG Endopeptidases
- The researchers identified the existence of two new proteins, or enzymes, which they named as IdeE2 and IdeZ2.
- These enzymes function as immunoglobulin G (IgG) endopeptidases, which have the capacity to break down antibodies. This characteristic is important as antibodies are the key elements in our immune response to infectious organisms like bacteria.
Comparative Analysis of New and Previously Known Enzymes
- IdeE2 and IdeZ2 showed significant sequence similarities with previously known IgG endopeptidases IdeE and IdeZ.
- What made the newly discovered enzymes stand out was their high substrate-specificity. This means they have a unique preference to interact with particular substances ─ in this case, horse immunoglobulin G (IgG).
- They fully cleave, or break down, horse IgG, while their activity against IgG from other animals including mouse, rabbit, cat, cow, sheep, and goat turned out low or non-existent.
Potential Usage in Vaccine Development
- The study evaluated the potential use of both originally known IdeE and the novel IdeE2 as vaccine components using mouse models.
- The results showed that both of these enzymes could induce immunity against S. equi ssp. equi infection. This essentially means they stimulated a protective immune response, suggesting they could be promising agents for vaccine development.
Cite This Article
APA
Hulting G, Flock M, Frykberg L, Lannergård J, Flock JI, Guss B.
(2009).
Two novel IgG endopeptidases of Streptococcus equi.
FEMS Microbiol Lett, 298(1), 44-50.
https://doi.org/10.1111/j.1574-6968.2009.01698.x Publication
Researcher Affiliations
- Department of Microbiology, Swedish University of Agricultural Sciences, Uppsala, Sweden.
MeSH Terms
- Amino Acid Sequence
- Animals
- Bacterial Proteins / genetics
- Bacterial Proteins / metabolism
- Bacterial Vaccines
- Cats
- Cattle
- DNA, Bacterial / chemistry
- DNA, Bacterial / genetics
- Endopeptidases / genetics
- Endopeptidases / immunology
- Endopeptidases / metabolism
- Goats
- Horses
- Immunoglobulin G / metabolism
- Lagomorpha
- Mice
- Molecular Sequence Data
- Rabbits
- Sequence Analysis, DNA
- Sequence Homology, Amino Acid
- Sheep
- Streptococcal Infections / immunology
- Streptococcal Infections / prevention & control
- Streptococcal Infections / veterinary
- Streptococcus equi / enzymology
- Substrate Specificity
Citations
This article has been cited 11 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.
- 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).
- Charbonneau ARL, Taylor E, Mitchell CJ, Robinson C, Cain AK, Leigh JA, Maskell DJ, Waller AS. Identification of genes required for the fitness of Streptococcus equi subsp. equi in whole equine blood and hydrogen peroxide.. Microb Genom 2020 Apr;6(4).
- 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.
- von Pawel-Rammingen U. Streptococcal IdeS and its impact on immune response and inflammation.. J Innate Immun 2012;4(2):132-40.
- 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.
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