IgA displays site- and subclass-specific glycoform differences despite equal glycoenzyme expression

IgA displays site- and subclass-specific glycoform differences despite equal glycoenzyme expression

Abstract Background Glycosylation is an important posttranslational modification of proteins and in most cases indispensable for proper protein function. Like most soluble proteins, IgA, the second most prevalent antibody in human serum, contains several N- and O-glycosylation sites. While for IgG t...

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Bibliographic Details
Main Authors: David Falck, Maria V. Sokolova, Carolien A. M. Koeleman, Vanessa Irumva, Philipp Kirchner, Sebastian R. Schulz, Katja G. Schmidt, Thomas Harrer, Arif B. Ekici, Bernd Spriewald, Georg Schett, Manfred Wuhrer, Martin Herrmann, Ulrike Steffen
Format: Article
Language:English
Published: BMC 2025-02-01
Series:Cell Communication and Signaling
Subjects:
IgA
Glycosylation
Glycoenzyme
Glycoform
Plasma cells
Online Access:https://doi.org/10.1186/s12964-025-02088-0

Internet

https://doi.org/10.1186/s12964-025-02088-0

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