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

Shadnezhad, Azadeh LU ; Naegeli, Andreas; Sjögren, Jonathan LU ; Adamczyk, Barbara; Leo, Fredrik; Allhorn, Maria LU ; Karlsson, Niclas G.; Jensen, Anders and Collin, Mattias LU (2016) In Future Microbiology 11(6). p.721-736
Abstract

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... (More)

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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Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
asparagine linked, chitinases, Endo-β-N-acetylglucosaminidase, glycosidase, IgG, Streptococcus dysgalactiae
in
Future Microbiology
volume
11
issue
6
pages
16 pages
publisher
Future Medicine Ltd.
external identifiers
  • Scopus:84971569538
ISSN
1746-0913
DOI
10.2217/fmb.16.14
language
English
LU publication?
yes
id
0547962c-b528-4307-8ce7-fe79bc3e1cd4
date added to LUP
2016-06-16 12:48:33
date last changed
2016-11-20 04:34:09
@misc{0547962c-b528-4307-8ce7-fe79bc3e1cd4,
  abstract     = {<p>Aim: The aim of this study was to identify and characterize EndoS-like enzymes in Streptococcus dysgalactiae subspecies dysgalactiae (SDSD). Materials &amp; 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.</p>},
  author       = {Shadnezhad, Azadeh and Naegeli, Andreas and Sjögren, Jonathan and Adamczyk, Barbara and Leo, Fredrik and Allhorn, Maria and Karlsson, Niclas G. and Jensen, Anders and Collin, Mattias},
  issn         = {1746-0913},
  keyword      = {asparagine linked,chitinases,Endo-β-N-acetylglucosaminidase,glycosidase,IgG,Streptococcus dysgalactiae},
  language     = {eng},
  month        = {06},
  number       = {6},
  pages        = {721--736},
  publisher    = {ARRAY(0x49a99e8)},
  series       = {Future Microbiology},
  title        = {EndoSd : An IgG glycan hydrolyzing enzyme in Streptococcus dysgalactiae subspecies dysgalactiae},
  url          = {http://dx.doi.org/10.2217/fmb.16.14},
  volume       = {11},
  year         = {2016},
}