[HTML][HTML] The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions
The human serum immunoglobulins IgG and IgA1 are produced in bone marrow and both
interact with specific cellular receptors that mediate biological events. In contrast to IgA1, the
glycosylation of IgG has been well characterized, and its interaction with various Fc
receptors (FcγRs) has been well studied. In this paper, we have analyzed the glycosylation
of IgA1 and IgA1 Fab and Fc as well as three recombinant IgA1 molecules, including twoN-
glycosylation mutants. Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge …
interact with specific cellular receptors that mediate biological events. In contrast to IgA1, the
glycosylation of IgG has been well characterized, and its interaction with various Fc
receptors (FcγRs) has been well studied. In this paper, we have analyzed the glycosylation
of IgA1 and IgA1 Fab and Fc as well as three recombinant IgA1 molecules, including twoN-
glycosylation mutants. Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge …