2004
DOI: 10.1111/j.1365-2249.2004.02442.x
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A dominant linear B-cell epitope of ricin A-chain is the target of a neutralizing antibody response in Hodgkin's lymphoma patients treated with an anti-CD25 immunotoxin

Abstract: Hodgkin's lymphoma patients treated with an anti-CD25 Ricin toxin A-chain (RTA)-based Immunotoxin (RFT5.dgA) develop an immune response against the toxic moiety of the immunoconjugate. The anti-RTA antibody response of 15 patients showing different clinical features and receiving different total amounts of RFT5.dgA was therefore studied in detail, considering antibody titre, IgG and IgM content, average binding efficacy and ability to inhibit in vitro the cytotoxicity of a RTA-based Immunotoxin. No correlation… Show more

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Cited by 50 publications
(56 citation statements)
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“…Antibodies elicited against either the ricin A (RTA) or B-chain can neutralize the toxin, although anti- bodies to the A-chain are superior in this respect [4,5]. The major human B-cell epitope for RTA has been identified by Castelletti et al [6] from cancer patients treated with a ricinconjugate immunotoxin, and lies within residues 161-175. Some innate immunity to oral exposure to ricin is provided by oligosaccharide chains of sIgA molecules lining the gut [7].…”
Section: Introductionmentioning
confidence: 99%
“…Antibodies elicited against either the ricin A (RTA) or B-chain can neutralize the toxin, although anti- bodies to the A-chain are superior in this respect [4,5]. The major human B-cell epitope for RTA has been identified by Castelletti et al [6] from cancer patients treated with a ricinconjugate immunotoxin, and lies within residues 161-175. Some innate immunity to oral exposure to ricin is provided by oligosaccharide chains of sIgA molecules lining the gut [7].…”
Section: Introductionmentioning
confidence: 99%
“…For use in humans, the ribosome-inactivating ability of RTA must be ablated. However, it is known that a number of immunodominant human T and B cell epitopes (at residues 161-175 and 174-185, respectively) lie immediately next to, or actually encompass, the active site (Tommasi et al, 2001;Castelletti et al, 2004). An approach in defining alternative vaccine candidates would therefore be to find RTA mutants with uncorrupted active sites that nevertheless display no or very low cytotoxic potency.…”
Section: Introductionmentioning
confidence: 99%
“…The mutant protein, Y80A/ V76M or RiVax, retains all the immunodominant epitopes recognized by a panel of monoclonal antibodies (MAbs) (16). In addition, the crystal structure of RiVax revealed no significant perturbation in the molecule (9), and all known immunodominant linear B cell and HLA class II-restricted T cell epitopes were retained (3,18). Without adjuvant, mice vaccinated intramuscularly (i.m.)…”
mentioning
confidence: 99%