Solution structure of deglycosylated human IgG1 shows the role of C_H2 glycans in its conformation.

ABSTRACT: The human immunoglobulin G (IgG) class is the most prevalent antibody in serum, with the IgG1 subclass being the most abundant. IgG1 is composed of two Fab regions connected to a Fc region through a 15-residue hinge peptide. Two glycan chains are conserved in the Fc region in IgG; however, their importance for the structure of intact IgG1 has remained unclear. Here, we subjected glycosylated and deglycosylated monoclonal human IgG1 (designated as A33) to a comparative multidisciplinary structural study of both forms. After deglycosylation using peptide:N-glycosidase F, analytical ultracentrifugation showed that IgG1 remained monomeric and the sedimentation coefficients s⁰_20,w of IgG1 decreased from 6.45 S by 0.16-0.27 S. This change was attributed to the reduction in

SUBMITTER: Spiteri VA 

PROVIDER: S-EPMC8204293 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature