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

被引：16
|
作者：
Shadnezhad, Azadeh [1 ]
Naegeli, Andreas [1 ]
Sjogren, Jonathan [1 ,2 ]
Adamczyk, Barbara [3 ]
Leo, Fredrik [1 ]
Allhorn, Maria [1 ]
Karlsson, Niclas G. [3 ]
Jensen, Anders [4 ]
Collin, Mattias [1 ]
机构：
[1] Lund Univ, Dept Clin Sci, Div Infect Med, Biomed Ctr B14, SE-22184 Lund, Sweden
[2] Genovis AB, Scheelevagen 2, SE-22007 Lund, Sweden
[3] Univ Gothenburg, Sahlgrenska Acad, Inst Biomed, Dept Med Biochem & Cell Biol, Gothenburg, Sweden
[4] Aarhus Univ, Fac Hlth Sci, Dept Biomed, Aarhus, Denmark
来源：
FUTURE MICROBIOLOGY | 2016年 / 11卷 / 06期
基金：
瑞典研究理事会; 瑞士国家科学基金会;
关键词：
asparagine linked; chitinases; Endo-beta-N-acetylglucosaminidase; glycosidase; IgG; Streptococcus dysgalactiae; EVOLUTIONARY CONSERVATION; IMMUNOGLOBULIN-G; LINKED GLYCANS; GLYCOSYLATION; ENDOGLYCOSIDASE; PYOGENES; ANTIBODIES; PROTEINS; RESIDUES; IGG1-FC;
D O I：
10.2217/fmb.16.14
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
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.
引用
收藏
页码：721 / 736
页数：16
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