Anti‐prostate immunotoxins: Cytotoxicity of E4 antibody–pseudomonas exotoxin constructs
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چکیده
منابع مشابه
Recombinant anti-erbB2 immunotoxins containing Pseudomonas exotoxin.
Immunotoxins were made using five different murine monoclonal antibodies to the human erbB2 gene product and LysPE40, a 40-kDa recombinant form of Pseudomonas exotoxin (PE) lacking its cell-binding domain. All five conjugates were specifically cytotoxic to cancer cell lines overexpressing erbB2 protein. The most active conjugate was e23-LysPE40, generated by chemical crosslinking of anti-erbB2 ...
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Serial evaluation in patients treated with a 10-day course of decitabine demonstrated higher BI 836858–mediated ADCC at day 28 post–decitabine therapy compared with pretreatment that was associated with significant upregulation of ligands to NK-activating receptor NKG2D (NKG2DL) in day 28 postdecitabine samples when compared with pretreatment. This study highlights 2 novel strategies relevant t...
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Pseudomonas exotoxin (PE) contains three domains whose functions are cell recognition, membrane translocation, and ADP ribosylation of elongation factor 2. PE40 is a form of PE which is missing the cell recognition domain. To study the properties of PE40, it was expressed in Escherichia coli using a vector which contains a T7 phage promoter, an OmpA signal sequence, and that portion of the PE g...
متن کاملProtection of the Furin Cleavage Site in Low-Toxicity Immunotoxins Based on Pseudomonas Exotoxin A
Recombinant immunotoxins (RITs) are fusions of an Fv-based targeting moiety and a toxin. Pseudomonas exotoxin A (PE) has been used to make several immunotoxins that have been evaluated in clinical trials. Immunogenicity of the bacterial toxin and off-target toxicity have limited the efficacy of these immunotoxins. To address these issues, we have previously made RITs in which the Fv is connecte...
متن کاملA variant of exotoxin A that forms potent and specific chemically conjugated immunotoxins.
To introduce a free sulfhydryl into Pseudomonas aeruginosa exotoxin A (ETA), methionine 161 in domain I of the toxin was changed to cysteine by site-directed mutagenesis. The free sulfhydryl provides a convenient site for covalent attachment of ETA to other proteins in the production of chimeric toxins. The mutation was then introduced into a variant of ETA that is impaired in receptor binding,...
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ژورنال
عنوان ژورنال: International Journal of Cancer
سال: 1998
ISSN: 0020-7136,1097-0215
DOI: 10.1002/(sici)1097-0215(19980703)77:1<123::aid-ijc19>3.3.co;2-v