The N-glycan Glycoprotein Deglycosylation Complex (Gpd) from Capnocytophaga canimorsus Deglycosylates Human IgG
2011
Deglycosylation of Human IgG by Capnocytophaga canimorsus
publication
Evidence: high
Author Information
Author(s): Renzi Francesco, Manfredi Pablo, Mally Manuela, Moes Suzette, Jenö Paul, Cornelis Guy R.
Primary Institution: Biozentrum der Universität Basel, Basel, Switzerland
Hypothesis
Can Capnocytophaga canimorsus deglycosylate human IgG?
Conclusion
Capnocytophaga canimorsus can deglycosylate human IgG, which may contribute to its pathogenicity.
Supporting Evidence
- Capnocytophaga canimorsus can deglycosylate human IgG.
- The Gpd complex is essential for the deglycosylation process.
- Deglycosylation may contribute to the pathogenicity of C. canimorsus.
- GpdG is identified as an endo-β-N-acetylglucosaminidase.
- Sialidase SiaC is involved in the deglycosylation process.
Takeaway
This study shows that a type of bacteria from dogs can remove sugar molecules from human antibodies, which might help it cause infections.
Methodology
The study involved genetic analysis, growth assays on human cells, and mass spectrometry to analyze glycosylation.
Digital Object Identifier (DOI)
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