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EndoSd: an IgG glycan hydrolyzing enzyme in Streptococcus dysgalactiae subspecies dysgalactiae

Journal article
Authors A. Shadnezhad
A. Naegeli
J. Sjogren
Barbara Adamczyk
F. Leo
M. Allhorn
Niclas G. Karlsson
A. Jensen
M. Collin
Published in Future Microbiology
Volume 11
Issue 6
Pages 721-736
ISSN 1746-0913
Publication year 2016
Published at Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 721-736
Language en
Keywords asparagine linked, chitinases, Endo-beta-N-acetylglucosaminidase, glycosidase, IgG, Streptococcus, evolutionary conservation, receptor interactions, immunoglobulin-g, linked glycans, glycosylation, endoglycosidase, pyogenes, antibodies, glomerulonephritis, deglycosylation, Microbiology
Subject categories Microbiology in the medical area


Aim: The aim of this study was to identify and characterize EndoS-like enzymes in Streptococcus dysgalactiae subspecies dysgalactiae (SDSD). Materials & methods: PCR, DNA sequencing, recombinant protein expression, lectin blot, ultra high performance liquid chromatography analysis and a chitinase assay were used to identify ndoS-like genes and characterize EndoSd. Results: EndoSd were found in four SDSD strains. EndoSd hydrolyzes the chitobiose core of the glycan on IgG. The amino acid sequence of EndoSd is 70% identical to EndoS in S. pyogenes, but it has a unique C-terminal sequence. EndoSd secretion is influenced by the carbohydrate composition of the growth medium. Conclusion: Our findings indicate that IgG glycan hydrolyzing activity is present in SDSD, and that the activity can be attributed to the here identified enzyme EndoSd.

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