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Immunotoxins: The Role of the Toxin

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TLDR
The utility of protein toxins, of both bacterial and plant origin, joined to antibodies for targeting cancer cells are discussed, both for treating human disease and probes of cellular function.
Abstract
Immunotoxins are antibody-toxin bifunctional molecules that rely on intracellular toxin action to kill target cells. Target specificity is determined via the binding attributes of the chosen antibody. Mostly, but not exclusively, immunotoxins are purpose-built to kill cancer cells as part of novel treatment approaches. Other applications for immunotoxins include immune regulation and the treatment of viral or parasitic diseases. Here we discuss the utility of protein toxins, of both bacterial and plant origin, joined to antibodies for targeting cancer cells. Finally, while clinical goals are focused on the development of novel cancer treatments, much has been learned about toxin action and intracellular pathways. Thus toxins are considered both medicines for treating human disease and probes of cellular function.

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Journal ArticleDOI

Advances in Anticancer Immunotoxin Therapy

TL;DR: A novel class of antibody-conjugated therapeutics currently in clinical development for a variety of malignancies that consist of an antibody-based targeting domain fused to a bacterial toxin payload for cell killing.
Journal ArticleDOI

Photonanomedicine: a convergence of photodynamic therapy and nanotechnology

TL;DR: The encouraging investigations that emphasize the potent synergy between photochemistry and nanotherapeutics, in addition to the growing realization of the value of these multi-faceted theranostic nanoplatforms, will assist in driving PNM formulations into mainstream oncological clinical practice as a necessary tool in the medical armamentarium.
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Immunotoxins for leukemia

TL;DR: Recombinant immunotoxins have been shown to be highly cytotoxic to leukemic blasts in vitro, in xenograft model systems, and in early-phase clinical trials in humans, and will likely play an increasing role in the treatment of leukemia.
Journal ArticleDOI

Peptide ligand-mediated targeted drug delivery of nanomedicines

TL;DR: Peptide ligands are advantageous over other classes of targeting ligands due to their accessibility of high-throughput screening, ease of synthesis, high specificity and affinity, etc.
Journal ArticleDOI

Immunotoxin: A new tool for cancer therapy.

TL;DR: Current trends and researches are ongoing on finding proteins that in combination with immunotoxins have minimal immunogenicity and the most potency for target cell killing.
References
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Journal ArticleDOI

Continuous cultures of fused cells secreting antibody of predefined specificity

TL;DR: The derivation of a number of tissue culture cell lines which secrete anti-sheep red blood cell (SRBC) antibodies is described here, made by fusion of a mouse myeloma and mouse spleen cells from an immunised donor.
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Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli.

TL;DR: A biosynthetic antibody binding site, which incorporated the variable domains of anti-digoxin monoclonal antibody 26-10 in a single polypeptide chain, was produced in Escherichia coli by protein engineering.
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Single-chain antigen-binding proteins

TL;DR: Three single-chain antigen-binding proteins are novel recombinant polypeptides, composed of an antibody variable light-chain amino acid sequence tethered to a variable heavy-chain sequence (VH) by a designed peptide that links the carboxyl terminus of the VL sequence to the amino terminusof the VH sequence.
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Derivation of specific antibody-producing tissue culture and tumor lines by cell fusion

TL;DR: Cell fusion techniques have been used to produce hybrids between myeloma cells and antibody‐producing cells that are permanently adapted to grow in tissue culture and are capable of inducing antibody-producing tumors in mice.
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One molecule of diphtheria toxin fragment A introduced into a cell can kill the cell.

TL;DR: Erythrocyte ghosts containing a known number of molecules of purified fragment A of diphtheria toxin with a constant amount of FITC-BSA as a fluorescence marker demonstrated that a single molecule of fragment A was sufficient to kill a cell.
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