| Literature DB >> 26216968 |
Andrew D Skora1, Jacqueline Douglass2, Michael S Hwang2, Ada J Tam3, Richard L Blosser3, Sandra B Gabelli4, Jianhong Cao5, Luis A Diaz2, Nickolas Papadopoulos2, Kenneth W Kinzler2, Bert Vogelstein6, Shibin Zhou7.
Abstract
Mutant epitopes encoded by cancer genes are virtually always located in the interior of cells, making them invisible to conventional antibodies. We here describe an approach to identify single-chain variable fragments (scFvs) specific for mutant peptides presented on the cell surface by HLA molecules. We demonstrate that these scFvs can be successfully converted to full-length antibodies, termed MANAbodies, targeting "Mutation-Associated Neo-Antigens" bound to HLA. A phage display library representing a highly diverse array of single-chain variable fragment sequences was first designed and constructed. A competitive selection protocol was then used to identify clones specific for mutant peptides bound to predefined HLA types. In this way, we obtained two scFvs, one specific for a peptide encoded by a common KRAS mutant and the other by a common epidermal growth factor receptor (EGFR) mutant. The scFvs bound to these peptides only when the peptides were complexed with HLA-A2 (KRAS peptide) or HLA-A3 (EGFR peptide). We converted one scFv to a full-length antibody (MANAbody) and demonstrate that the MANAbody specifically reacts with mutant peptide-HLA complex even when the peptide differs by only one amino acid from the normal, WT form.Entities:
Keywords: antibody engineering; immunotherapy; oncogene; personalized; therapy
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Year: 2015 PMID: 26216968 PMCID: PMC4538619 DOI: 10.1073/pnas.1511996112
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205