Short reportsPhage libraries for generation of clinically useful antibodies
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Cited by (164)
Nanoparticles and trained immunity: Glimpse into the future
2021, Advanced Drug Delivery ReviewsRapid de novo generation of antigen specific human B cells with expression of Blimp‐1 and AID by in vitro immunization
2017, Experimental Cell ResearchCitation Excerpt :It was shown that repeated injections of non-human antibodies led to a strong immune response that significantly limited or undermined their therapeutic efficacy [2,4,6]. Hence, full human mAbs have since emerged as a result of several approaches, including the phage display method and transgenic mouse system with an entire human antibody repertoire [7–12]. However, transgenic mouse system is lengthy and costly.
Plasma half-life extension of small recombinant antibodies by fusion to immunoglobulin-binding domains
2012, Journal of Biological ChemistryCitation Excerpt :Results are shown as mean value ± S.D. ScDb-IgBD and scFv-IgBD fusion proteins were generated by fusing IgBDs from SpA, SpG, or PpL to the C terminus of a bispecific single-chain diabody directed against CEA and CD3 (scDb CEACD3) or a single-chain Fv directed against CEA (scFv CEA) (17) (Fig. 2a). From SpA we used domain B (18), domain D (9), and a modified version of domain E, which was described to exhibit increased thermal stability (19).
Establishing a knowledge trail from molecular experiments to clinical trials
2011, New BiotechnologyConvergent potency of internalized gelonin immunotoxins across varied cell lines, antigens, and targeting moieties
2011, Journal of Biological ChemistryCitation Excerpt :MFE-23 is an antibody single-chain variable fragment (scFv) directed against CEA. Originally identified by phage library selection, this scFv was later humanized by resurfacing and engineered in yeast for greater stability and solubility (shMFE) as well as affinity (sm3E) (31–33). Both of these engineered molecules are well expressed in yeast and have Kd values of ∼7 nm and ∼30 pm, respectively.