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Göteborgs universitets publikationer

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

Författare och institution:
A. Shadnezhad (-); A. Naegeli (-); J. Sjogren (-); Barbara Adamczyk (Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi); F. Leo (-); M. Allhorn (-); Niclas G. Karlsson (Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi); A. Jensen (-); M. Collin (-)
Publicerad i:
Future Microbiology, 11 ( 6 ) s. 721-736
ISSN:
1746-0913
Publikationstyp:
Artikel, refereegranskad vetenskaplig
Publiceringsår:
2016
Språk:
engelska
Fulltextlänk:
Sammanfattning (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.
Ämne (baseras på Högskoleverkets indelning av forskningsämnen):
MEDICIN OCH HÄLSOVETENSKAP ->
Medicinska grundvetenskaper ->
Mikrobiologi inom det medicinska området
Nyckelord:
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
Postens nummer:
238303
Posten skapad:
2016-06-27 10:38
Posten ändrad:
2016-06-27 10:39

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