{"database":"biostudies-literature","file_versions":[],"scores":{"citationCount":0,"reanalysisCount":0,"viewCount":53,"searchCount":0},"additional":{"submitter":["Tateno H"],"funding":["NCHHSTP CDC HHS"],"pagination":["811-20"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4437484"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["4(5)"],"pubmed_abstract":["The application of stem-cell-based therapies in regenerative medicine is hindered by the tumorigenic potential of residual human pluripotent stem cells. Previously, we identified a human pluripotent stem-cell-specific lectin probe, called rBC2LCN, by comprehensive glycome analysis using high-density lectin microarrays. Here we developed a recombinant lectin-toxin fusion protein of rBC2LCN with a catalytic domain of Pseudomonas aeruginosa exotoxin A, termed rBC2LCN-PE23, which could be expressed as a soluble form from the cytoplasm of Escherichia coli and purified to homogeneity by one-step affinity chromatography. rBC2LCN-PE23 bound to human pluripotent stem cells, followed by its internalization, allowing intracellular delivery of a cargo of cytotoxic protein. The addition of rBC2LCN-PE23 to the culture medium was sufficient to completely eliminate human pluripotent stem cells. Thus, rBC2LCN-PE23 has the potential to contribute to the safety of stem-cell-based therapies."],"journal":["Stem cell reports"],"pubmed_title":["Elimination of tumorigenic human pluripotent stem cells by a recombinant lectin-toxin fusion protein."],"pmcid":["PMC4437484"],"funding_grant_id":["UA1 PS000063"],"pubmed_authors":["Saito S","Shimizu M","Asashima M","Tateno H","Minoshima F","Hirabayashi J","Onuma Y","Ito Y","Aiki Y"],"view_count":["53"],"additional_accession":[]},"is_claimable":false,"name":"Elimination of tumorigenic human pluripotent stem cells by a recombinant lectin-toxin fusion protein.","description":"The application of stem-cell-based therapies in regenerative medicine is hindered by the tumorigenic potential of residual human pluripotent stem cells. Previously, we identified a human pluripotent stem-cell-specific lectin probe, called rBC2LCN, by comprehensive glycome analysis using high-density lectin microarrays. Here we developed a recombinant lectin-toxin fusion protein of rBC2LCN with a catalytic domain of Pseudomonas aeruginosa exotoxin A, termed rBC2LCN-PE23, which could be expressed as a soluble form from the cytoplasm of Escherichia coli and purified to homogeneity by one-step affinity chromatography. rBC2LCN-PE23 bound to human pluripotent stem cells, followed by its internalization, allowing intracellular delivery of a cargo of cytotoxic protein. The addition of rBC2LCN-PE23 to the culture medium was sufficient to completely eliminate human pluripotent stem cells. Thus, rBC2LCN-PE23 has the potential to contribute to the safety of stem-cell-based therapies.","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 May","modification":"2024-11-09T12:57:56.313Z","creation":"2019-03-27T01:51:52Z"},"accession":"S-EPMC4437484","cross_references":{"pubmed":["25866158"],"doi":["10.1016/j.stemcr.2015.02.016"]}}