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

Azadeh Shadnezhad; Andreas Nägeli; Jonathan Sjögren; Barbara Adamczyk; Fredrik Leo; Maria Allhorn; Niclas G. Karlsson; Anders Jensen; Mattias Collin

doi:10.2217/fmb.16.14

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

Azadeh Shadnezhad, Andreas Nägeli, Jonathan Sjögren, Barbara Adamczyk, Fredrik Leo, Maria Allhorn, Niclas G. Karlsson, Anders Jensen, Mattias Collin

Research output: Contribution to journal › Article › peer-review

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 activity is present in SDSD, and that the activity can be attributed to the here identified enzyme EndoSd.

Original language	English
Pages (from-to)	721-736
Number of pages	16
Journal	Future Microbiology
Volume	11
Issue number	6
DOIs	https://doi.org/10.2217/fmb.16.14
Publication status	Published - 2016 Jun 1

Subject classification (UKÄ)

Infectious Medicine
Cell and Molecular Biology

Free keywords

asparagine linked
chitinases
Endo-β-N-acetylglucosaminidase
glycosidase
IgG
Streptococcus dysgalactiae

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10.2217/fmb.16.14Licence: CC BY-NC-ND

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title = "EndoSd: An IgG glycan hydrolyzing enzyme in Streptococcus dysgalactiae subspecies dysgalactiae",

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 activity is present in SDSD, and that the activity can be attributed to the here identified enzyme EndoSd.",

keywords = "asparagine linked, chitinases, Endo-β-N-acetylglucosaminidase, glycosidase, IgG, Streptococcus dysgalactiae",

author = "Azadeh Shadnezhad and Andreas N{\"a}geli and Jonathan Sj{\"o}gren and Barbara Adamczyk and Fredrik Leo and Maria Allhorn and Karlsson, {Niclas G.} and Anders Jensen and Mattias Collin",

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month = jun,

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doi = "10.2217/fmb.16.14",

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T2 - An IgG glycan hydrolyzing enzyme in Streptococcus dysgalactiae subspecies dysgalactiae

AU - Shadnezhad, Azadeh

AU - Nägeli, Andreas

AU - Sjögren, Jonathan

AU - Adamczyk, Barbara

AU - Leo, Fredrik

AU - Allhorn, Maria

AU - Karlsson, Niclas G.

AU - Jensen, Anders

AU - Collin, Mattias

PY - 2016/6/1

Y1 - 2016/6/1

N2 - 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.

AB - 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.

KW - asparagine linked

KW - chitinases

KW - Endo-β-N-acetylglucosaminidase

KW - glycosidase

KW - IgG

KW - Streptococcus dysgalactiae

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DO - 10.2217/fmb.16.14

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AN - SCOPUS:84971569538

SN - 1746-0913

VL - 11

SP - 721

EP - 736

JO - Future Microbiology

JF - Future Microbiology

IS - 6

ER -

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

Abstract

Subject classification (UKÄ)

Free keywords

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Bacterial IgG Modulating Endoglycosidases. Basic biology and biotechnological applications.

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