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Proteolytic processing of the streptococcal IgG cleaving enzyme IdeS reduces immunorecognition without affecting the biological activity of the enzyme
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
(English)Manuscript (preprint) (Other academic)
National Category
Microbiology in the medical area
Identifiers
URN: urn:nbn:se:umu:diva-54050OAI: oai:DiVA.org:umu-54050DiVA: diva2:515377
Available from: 2012-04-12 Created: 2012-04-12 Last updated: 2012-04-12Bibliographically approved
In thesis
1. The streptococcal IgG degrading enzyme IdeS: studies on host-pathogen interactions
Open this publication in new window or tab >>The streptococcal IgG degrading enzyme IdeS: studies on host-pathogen interactions
2012 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The important human pathogen Streptococcus pyogenes causes both mild infections such as pharyngitis and impetigo but also severe life threatening invasive infections.  Specific antibodies (IgG) recognize pathogens and are important mediators for pathogen clearance by the immune defence. S.ipyogenes expresses a highly effective and specific IgG endopeptidase called IdeS (immunoglobulin degrading enzyme of S.ipyogenes). IdeS rescues bacteria from opsonising IgG by cleavage of IgG generating two fragments F(ab´)2 and ½Fc. Moreover, IdeS block ROS production by neutrophils. In this thesis I have studied (i) allelic variants of IdeS and their biological potential, (ii) consequences of ½Fc production for host-pathogen interactions and (iii) IdeS processing by streptococcal and neutrophil proteases.

When investigating the allelic variants of IdeS we could show that in respect to IgG degradation and inhibition of ROS production the allelic variants where indistinguishable, however the allelic variant of serotype M28 appears to be an unique exception as this protein was deficient in IgG cleavage but still inhibited ROS production. Further, the ½Fc fragments produced when IgG is cleaved by IdeS were shown to prime human neutrophils and under ex vivo experimental conditions this increased the bactericidal activity of the neutrophils. Finally, we made the interesting finding that IdeS is N-terminally processed by neutrophil proteases and by the streptococcal protease SpeB, but retain enzymatic activity and was less immunogenic compared to the full length protein.

Place, publisher, year, edition, pages
Umeå: Umeå universitet, 2012. 43 p.
Series
Umeå University medical dissertations, ISSN 0346-6612 ; 1491
Keyword
streptococcus pyogenes, IdeS
National Category
Microbiology
Research subject
Molecular Biology
Identifiers
urn:nbn:se:umu:diva-53706 (URN)978-91-7459-404-1 (ISBN)
Public defence
2012-05-03, Bergasalen, NUS By 27, Umeå, 10:00 (English)
Opponent
Supervisors
Available from: 2012-04-12 Created: 2012-04-04 Last updated: 2012-05-16Bibliographically approved

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Persson, HelenaJohansson Söderberg, JennyVindebro, Reinevon Pawel-Rammingen, Ulrich
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