Toward clinical use of the IgG specific enzymes IdeS and EndoS against antibody-mediated diseases
Collin, Mattias LU
and Björck, Lars
LU
(2017)
In Methods in Molecular Biology
1535.
p.339-351
- Abstract
The endoglycosidase EndoS and the protease IdeS from the human pathogen Streptococcus pyogenes are immunomodulating enzymes hydrolyzing human IgG. IdeS cleaves IgG in the lower hinge region, while EndoS hydrolyzes the conserved N-linked glycan in the Fc region. Both enzymes are remarkably specific for human IgG that after hydrolysis loses most of its effector functions, such as binding to leukocytes and complement activation, all contributing to bacterial evasion of adaptive immunity. However, taken out of their infectious context, we and others have shown that IdeS and EndoS can alleviate autoimmune disease in a number of animal models of antibody-mediated disorders. In this chapter, we will briefly describe the discovery and... (More)
The endoglycosidase EndoS and the protease IdeS from the human pathogen Streptococcus pyogenes are immunomodulating enzymes hydrolyzing human IgG. IdeS cleaves IgG in the lower hinge region, while EndoS hydrolyzes the conserved N-linked glycan in the Fc region. Both enzymes are remarkably specific for human IgG that after hydrolysis loses most of its effector functions, such as binding to leukocytes and complement activation, all contributing to bacterial evasion of adaptive immunity. However, taken out of their infectious context, we and others have shown that IdeS and EndoS can alleviate autoimmune disease in a number of animal models of antibody-mediated disorders. In this chapter, we will briefly describe the discovery and characterization of these unique enzymes, present the findings from a number of animal models of autoimmunity where the enzymes have been tested, and outline the ongoing clinical testing of IdeS. Furthermore, we will discuss the rationale for further development of IdeS and EndoS into novel pharmaceuticals against diseases where IgG antibodies contribute to the pathology, including, but not restricted to, chronic and acute autoimmunity, transplant rejection, and antidrug antibody reactions.
(Less)
- author
- Collin, Mattias
LU
and Björck, Lars
LU
- organization
- publishing date
- 2017
- type
- Chapter in Book/Report/Conference proceeding
- publication status
- published
- subject
- keywords
- Autoimmunity, Glycan hydrolysis, Glycosylation, Immune evasion, Immunoglobulins, Proteases, Transplant rejection
- host publication
- Methods in Molecular Biology
- series title
- Methods in Molecular Biology
- volume
- 1535
- pages
- 13 pages
- publisher
- Humana Press
- external identifiers
-
- scopus:85005950992
- pmid:27914091
- ISSN
- 10643745
- DOI
- 10.1007/978-1-4939-6673-8_23
- language
- English
- LU publication?
- yes
- id
- e8c5ecc3-317f-4fed-8fbd-0a529f5a39ac
- date added to LUP
- 2017-03-16 14:08:08
- date last changed
- 2024-10-14 02:47:39
@inbook{e8c5ecc3-317f-4fed-8fbd-0a529f5a39ac,
abstract = {{<p>The endoglycosidase EndoS and the protease IdeS from the human pathogen Streptococcus pyogenes are immunomodulating enzymes hydrolyzing human IgG. IdeS cleaves IgG in the lower hinge region, while EndoS hydrolyzes the conserved N-linked glycan in the Fc region. Both enzymes are remarkably specific for human IgG that after hydrolysis loses most of its effector functions, such as binding to leukocytes and complement activation, all contributing to bacterial evasion of adaptive immunity. However, taken out of their infectious context, we and others have shown that IdeS and EndoS can alleviate autoimmune disease in a number of animal models of antibody-mediated disorders. In this chapter, we will briefly describe the discovery and characterization of these unique enzymes, present the findings from a number of animal models of autoimmunity where the enzymes have been tested, and outline the ongoing clinical testing of IdeS. Furthermore, we will discuss the rationale for further development of IdeS and EndoS into novel pharmaceuticals against diseases where IgG antibodies contribute to the pathology, including, but not restricted to, chronic and acute autoimmunity, transplant rejection, and antidrug antibody reactions.</p>}},
author = {{Collin, Mattias and Björck, Lars}},
booktitle = {{Methods in Molecular Biology}},
issn = {{10643745}},
keywords = {{Autoimmunity; Glycan hydrolysis; Glycosylation; Immune evasion; Immunoglobulins; Proteases; Transplant rejection}},
language = {{eng}},
pages = {{339--351}},
publisher = {{Humana Press}},
series = {{Methods in Molecular Biology}},
title = {{Toward clinical use of the IgG specific enzymes IdeS and EndoS against antibody-mediated diseases}},
url = {{http://dx.doi.org/10.1007/978-1-4939-6673-8_23}},
doi = {{10.1007/978-1-4939-6673-8_23}},
volume = {{1535}},
year = {{2017}},
}