An immunodominant CTL epitope expressed by in vitro transformed cells is derived from plasmid vector backbone sequences

Hall, Thorbald van; Rhee, N. van de; Schoenberger, Stephen P.; Vierboom, Michel; Verreck, Frank A. W.; Melief, Cornelis J.M.; Offringa, Rienk

doi:10.1016/s0165-2478(97)88863-3

Cited by 1 publication

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“…The peptide RAHYNIVTF (49)(50)(51)(52)(53)(54)(55)(56)(57) (1 kDa) derived from human papilloma virus-16 (HPV) E7 protein (Genescript, Piscataway, NJ) was loaded onto the RAH antigen by in vitro refolding to create a peptide-presenting MHC (pMHC) antigen that was purified by size exclusion chromatography [46]. This HPV-induced RAHYNIVTF peptide is common in ovarian cancers and is known to induce a T-cell response when presented by H-2D b in the mouse [45,47,48]. To target the RAH antigen, monoclonal antibodies with T-cell receptor-like specificity anti-RAH (TCRmAbs) (150 kDa) were generated by classical B cell hybridoma technology [40].…”

Section: Generation and Validation Of Antigens And Antibodiesmentioning

confidence: 99%

“…To target the RAH antigen, monoclonal antibodies with T-cell receptor-like specificity anti-RAH (TCRmAbs) (150 kDa) were generated by classical B cell hybridoma technology [40]. These TCRmAbs specifically recognize RAH/ H-2D b pMHCs to form complexes [47]. A different TCRmAb specifically targeting a West Nile virus peptide (anti-WNV, 150 kDa) presented by H-2D b pMHC [49] was used as negative control.…”

Section: Generation and Validation Of Antigens And Antibodiesmentioning

confidence: 99%

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Detection of specific antibody-ligand interactions with a self-induced back-action actuated nanopore electrophoresis sensor

et al. 2019

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Recent advances in plasmonic nanopore technologies have enabled the use of concurrently acquired bimodal optical-electrical data for improved quantification of molecular interactions. This work presents the use of a new plasmonic nanosensor employing self-induced back-action (SIBA) for optical trapping to enable SIBA-actuated nanopore electrophoresis (SANE) for quantifying antibody-ligand interactions. T-cell receptor-like antibodies (TCRmAbs) engineered to target peptide-presenting major histocompatibility complex (pMHC) ligands, representing a model of target ligands presented on the surface of cancer cells, were used to test the SANE sensor's ability to identify specific antibody-ligand binding. Cancer-irrelevant TCRmAbs targeting the same pMHCs were also tested as a control. It was found that the sensor could provide bimodal molecular signatures that could differentiate between antibody, ligand and the complexes that they formed, as well as distinguish between specific and non-specific interactions. Furthermore, the results suggested an interesting phenomenon of increased antibody-ligand complex bound fraction detected by the SANE sensor compared to that expected for corresponding bulk solution concentrations. A possible physical mechanism and potential advantages for the sensor's ability to augment complex formation near its active sensing volume at concentrations lower than the free solution equilibrium binding constant (K D ) are discussed.

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