Mutational deglycosylation of the Fc portion of immunoglobulin G causes O-sulfation of tyrosine adjacently preceding the originally glycosylated site

Research output: Contribution to journalArticle

Authors

Colleges, School and Institutes

Abstract

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.

Details

Original languageEnglish
Pages (from-to)3474-3479
Number of pages6
JournalFEBS Letters
Volume584
Issue number15
Publication statusPublished - 1 Aug 2010

Keywords

  • N-Glycosylation, Fc, IgG, Mass spectrometry, Tyrosine sulfation