Abstract
The deglycosylation of immunoglobulin G (IgG) antibodies with the bacterial enzyme EndoS has been suggested as a potential treatment for some autoimmune disorders as this process leads to a diminished immune response. The reduction in immune response is thought to arise from weakened binding of effector molecules to the fragment crystallizable (Fc) region of IgG antibodies as a result of a conformational change in the Fc region. The nature of this structural alteration is uncertain due to conflicting results obtained from x-ray crystallography and small-angle x-ray scattering studies. To further examine the impact of deglycosylation on the structure of the Fc region, we have examined both glycosylated and EndoS deglycosylated IgG antibodies using single molecule Forster Resonance Energy Transfer (smFRET). The FRET efficiency histograms obtained from studying freely-diffusing, dye-labeled antibodies suggest that the flexibility of the Fc region increases upon deglycosylation.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.