{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhang X"],"funding":["National Institute of Allergy and Infectious Diseases","NIDDK NIH HHS","NIAID NIH HHS","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["3013-3023"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9492806"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(11)"],"pubmed_abstract":["Lysosome-targeting chimeras (LYTACs) offer an opportunity for the degradation of extracellular and membrane-associated proteins of interest. Here, we report an efficient chemoenzymatic method that enables a single-step and site-specific conjugation of high-affinity mannose-6-phosphate (M6P) glycan ligands to antibodies without the need of protein engineering and conventional click reactions that would introduce \"unnatural\" moieties, yielding homogeneous antibody-M6P glycan conjugates for targeted degradation of membrane-associated proteins. Using trastuzumab and cetuximab as model antibodies, we showed that the wild-type endoglycosidase S (Endo-S) could efficiently perform the antibody deglycosylation and simultaneous transfer of an M6P-glycan from a synthetic M6P-glycan oxazoline to the d"],"journal":["ACS chemical biology"],"pubmed_title":["Site-Specific Chemoenzymatic Conjugation of High-Affinity M6P Glycan Ligands to Antibodies for Targeted Protein Degradation."],"pmcid":["PMC9492806"],"funding_grant_id":["R01AI155716","R01 GM096973","R01GM096973","R01 AI155716","R01 DK119937"],"pubmed_authors":["Liu H","He J","Donahue TC","Muthana MM","Zhang X","Wang LX","Su L","Ou C"],"additional_accession":[]},"is_claimable":false,"name":"Site-Specific Chemoenzymatic Conjugation of High-Affinity M6P Glycan Ligands to Antibodies for Targeted Protein Degradation.","description":"Lysosome-targeting chimeras (LYTACs) offer an opportunity for the degradation of extracellular and membrane-associated proteins of interest. Here, we report an efficient chemoenzymatic method that enables a single-step and site-specific conjugation of high-affinity mannose-6-phosphate (M6P) glycan ligands to antibodies without the need of protein engineering and conventional click reactions that would introduce \"unnatural\" moieties, yielding homogeneous antibody-M6P glycan conjugates for targeted degradation of membrane-associated proteins. Using trastuzumab and cetuximab as model antibodies, we showed that the wild-type endoglycosidase S (Endo-S) could efficiently perform the antibody deglycosylation and simultaneous transfer of an M6P-glycan from a synthetic M6P-glycan oxazoline to the d","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Nov","modification":"2025-04-25T19:58:38.801Z","creation":"2025-04-06T08:14:09.355Z"},"accession":"S-EPMC9492806","cross_references":{"pubmed":["35316032"],"doi":["10.1021/acschembio.1c00751"]}}