{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Fleming BD"],"funding":["Intramural NIH HHS","National Cancer Institute","NCI NIH HHS"],"pagination":["1696-1711"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7069773"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["71(5)"],"pubmed_abstract":["<h4>Background and aims</h4>Treatment of hepatocellular carcinomas using our glypican-3 (GPC3)-targeting human nanobody (HN3) immunotoxins causes potent tumor regression by blocking protein synthesis and down-regulating the Wnt signaling pathway. However, immunogenicity and a short serum half-life may limit the ability of immunotoxins to transition to the clinic.<h4>Approach and results</h4>To address these concerns, we engineered HN3-based immunotoxins to contain various deimmunized Pseudomonas exotoxin (PE) domains. This included HN3-T20, which was modified to remove T-cell epitopes and contains a PE domain II truncation. We compared them to our previously reported B-cell deimmunized immunotoxin (HN3-mPE24) and our original HN3-immunotoxin with a wild-type PE domain (HN3-PE38). All of ou"],"journal":["Hepatology (Baltimore, Md.)"],"pubmed_title":["Engineered Anti-GPC3 Immunotoxin, HN3-ABD-T20, Produces Regression in Mouse Liver Cancer Xenografts Through Prolonged Serum Retention."],"pmcid":["PMC7069773"],"funding_grant_id":["Z01 BC010891","ZIA BC010891"],"pubmed_authors":["Pastan I","Hall MD","Fleming BD","Greten TF","Ho M","Longerich T","Urban DJ"],"additional_accession":[]},"is_claimable":false,"name":"Engineered Anti-GPC3 Immunotoxin, HN3-ABD-T20, Produces Regression in Mouse Liver Cancer Xenografts Through Prolonged Serum Retention.","description":"<h4>Background and aims</h4>Treatment of hepatocellular carcinomas using our glypican-3 (GPC3)-targeting human nanobody (HN3) immunotoxins causes potent tumor regression by blocking protein synthesis and down-regulating the Wnt signaling pathway. However, immunogenicity and a short serum half-life may limit the ability of immunotoxins to transition to the clinic.<h4>Approach and results</h4>To address these concerns, we engineered HN3-based immunotoxins to contain various deimmunized Pseudomonas exotoxin (PE) domains. This included HN3-T20, which was modified to remove T-cell epitopes and contains a PE domain II truncation. We compared them to our previously reported B-cell deimmunized immunotoxin (HN3-mPE24) and our original HN3-immunotoxin with a wild-type PE domain (HN3-PE38). All of ou","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 May","modification":"2025-04-05T10:07:25.668Z","creation":"2022-02-09T18:10:11.439Z"},"accession":"S-EPMC7069773","cross_references":{"pubmed":["31520528"],"doi":["10.1002/hep.30949"]}}