{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["van der Kaaij A"],"funding":["The International Coordination of Research on Infectious Animal Diseases","Eurostars","Netherlands Organisation for Scientific Research, Veni grant","Dutch Research Council (NWO)","The center for unusual collaboration (CUCo)"],"pagination":["224-238"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12854890"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["24(1)"],"pubmed_abstract":["Glycosylation is an important aspect for many biopharmaceuticals, including vaccines against parasitic helminths. Plants, especially Nicotiana benthamiana, have proven to be excellent production hosts for biopharmaceuticals with tailor-made glycosylation. If desired, galactosylation can be introduced on biopharmaceuticals through co-expression of the appropriate glycosyltransferase. However, achieving homogenous glycoforms with terminal galactose residues remains difficult as native N. benthamiana β-galactosidases (NbBGALs) truncate these glycans. Recently, the first NbBGAL has been identified, but a knockout line was insufficient to achieve near complete galactosylation, suggesting that other enzymes could have similar activity. In this study, we selected 10 NbBGALs for further investigat"],"journal":["Plant biotechnology journal"],"pubmed_title":["Identification of β-galactosidases along the secretory pathway of Nicotiana benthamiana that collectively hamper engineering of galactose-extended glycans on recombinant glycoproteins."],"pmcid":["PMC12854890"],"funding_grant_id":["16740","E! 115017"],"pubmed_authors":["Bunte MJM","Mokhtari S","Schots A","Wilbers RHP","Nijhof L","Nibbering P","van der Kaaij A","Overmars H"],"additional_accession":[]},"is_claimable":false,"name":"Identification of β-galactosidases along the secretory pathway of Nicotiana benthamiana that collectively hamper engineering of galactose-extended glycans on recombinant glycoproteins.","description":"Glycosylation is an important aspect for many biopharmaceuticals, including vaccines against parasitic helminths. Plants, especially Nicotiana benthamiana, have proven to be excellent production hosts for biopharmaceuticals with tailor-made glycosylation. If desired, galactosylation can be introduced on biopharmaceuticals through co-expression of the appropriate glycosyltransferase. However, achieving homogenous glycoforms with terminal galactose residues remains difficult as native N. benthamiana β-galactosidases (NbBGALs) truncate these glycans. Recently, the first NbBGAL has been identified, but a knockout line was insufficient to achieve near complete galactosylation, suggesting that other enzymes could have similar activity. In this study, we selected 10 NbBGALs for further investigat","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-06-09T06:47:30.796Z","creation":"2026-06-09T03:11:52.113Z"},"accession":"S-EPMC12854890","cross_references":{"pubmed":["40333706"],"doi":["10.1111/pbi.70126"]}}