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Proteolytic processing of the streptococcal IgG endopeptidase IdeS modulates the functional properties of the enzyme and results in reduced immunorecognition
Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR). Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten).
Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR). Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten).
Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR). Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten).
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2015 (engelsk)Inngår i: Molecular Immunology, ISSN 0161-5890, E-ISSN 1872-9142, Vol. 68, nr 2, s. 176-184Artikkel i tidsskrift (Fagfellevurdert) Published
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Abstract [en]

The important human gram positive bacterial pathogen Streptococcus pyogenes employs various virulence factors to promote inflammation and to facilitate invasive disease progression. In this study we explored the relation of the secreted streptococcal cysteine proteases IdeS and SpeB, and neutrophil (PMN) proteases. We found that SpeB is resistant to proteolytic attack in an inflammatory environment, emphasizing the importance of SpeB for streptococcal pathogenicity, while PMN enzymes and SpeB itself process the IgG degrading endopeptidase IdeS. Processing occurs as NH2-terminal cleavage of IdeS resulting in reduced immunorecognition of the protease by specific antibodies. While the endopeptidase retains IgG cleaving activity, its ability to suppress the generation of reactive oxygen species is abolished. We suggest that the cleavage of NH2-terminal peptides by SpeB and/or neutrophil proteases is a mechanism evolved to prevent early inactivation of this important streptococcal virulence factor, albeit at the cost of impaired functionality.

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Elsevier, 2015. Vol. 68, nr 2, s. 176-184
Emneord [en]
Neutrophil proteases, S. pyogenes, Cysteine protease, SpeB, IdeS, ROS
HSV kategori
Identifikatorer
URN: urn:nbn:se:umu:diva-114635DOI: 10.1016/j.molimm.2015.07.014ISI: 000366767700122PubMedID: 26343448OAI: oai:DiVA.org:umu-114635DiVA, id: diva2:900254
Tilgjengelig fra: 2016-02-03 Laget: 2016-01-25 Sist oppdatert: 2018-06-07bibliografisk kontrollert

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

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