{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ruocco V"],"funding":["NCI NIH HHS","NIGMS NIH HHS"],"pagination":["1390659"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11026580"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11"],"pubmed_abstract":["The transition of IgA antibodies into clinical development is crucial because they have the potential to create a new class of therapeutics with superior pathogen neutralization, cancer cell killing, and immunomodulation capacity compared to IgG. However, the biological role of IgA glycans in these processes needs to be better understood. This study provides a detailed biochemical, biophysical, and structural characterization of recombinant monomeric human IgA2, which varies in the amount/locations of attached glycans. Monomeric IgA2 antibodies were produced by removing the <i>N</i>-linked glycans in the CH1 and CH2 domains. The impact of glycans on oligomer formation, thermal stability, and receptor binding was evaluated. In addition, we performed a structural analysis of recombinant IgA2"],"journal":["Frontiers in molecular biosciences"],"pubmed_title":["Effects of <i>N</i>-glycans on the structure of human IgA2."],"pmcid":["PMC11026580"],"funding_grant_id":["P30 GM124169","P01 CA092584"],"pubmed_authors":["Rad B","Tscheliessnig R","Grunwald-Gruber C","Strasser R","Ruocco V","Hammel M"],"additional_accession":[]},"is_claimable":false,"name":"Effects of <i>N</i>-glycans on the structure of human IgA2.","description":"The transition of IgA antibodies into clinical development is crucial because they have the potential to create a new class of therapeutics with superior pathogen neutralization, cancer cell killing, and immunomodulation capacity compared to IgG. However, the biological role of IgA glycans in these processes needs to be better understood. This study provides a detailed biochemical, biophysical, and structural characterization of recombinant monomeric human IgA2, which varies in the amount/locations of attached glycans. Monomeric IgA2 antibodies were produced by removing the <i>N</i>-linked glycans in the CH1 and CH2 domains. The impact of glycans on oligomer formation, thermal stability, and receptor binding was evaluated. In addition, we performed a structural analysis of recombinant IgA2","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024","modification":"2026-04-08T15:28:54.688Z","creation":"2026-04-08T04:46:51.428Z"},"accession":"S-EPMC11026580","cross_references":{"pubmed":["38645274"],"doi":["10.3389/fmolb.2024.1390659"]}}