Journal
FEBS LETTERS
Volume 584, Issue 15, Pages 3474-3479Publisher
WILEY
DOI: 10.1016/j.febslet.2010.07.004
Keywords
IgG; Tyrosine sulfation; N-Glycosylation; Fc; Mass spectrometry
Funding
- Bruker Daltonics Japan
- Bruker Daltonik GmbH
- Ministry of Education, Culture, Sports, Science and Technology (MEXT)
- National Institute of Biomedical Innovation (NIBIO)
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Mutagenesis directed to a specific glycosylation site has been widely used to examine biological roles of individual glycans. However, occurrence of any post-translational modification on such deglycosylated mutants has not yet been well characterized. Here we performed mass spectrometric analyses of the Fc fragment of an unglycosylated mutant of mouse immunoglobulin G2b, whose conserved N-glycosylation site, i.e. Asn297, was substituted with alanine. We found that a major part of this mutant is sulfated at Tyr296, which adjacently precedes the originally glycosylated site. Our findings demonstrate that mutational deglycosylation can induce an unexpected post-translational modification in the protein. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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