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Characterization of anti-ricin monoclonal antibodies and the construction of a chimeric murine-human IgG2/K anti-ricin monoclonal antibody

Ricin toxin is a very deadly plant protein that is synthesized by the plant Ricinus communis. The molecular structure of ricin toxin places it in a group of similar proteins classified as a Type II RIP due to its heterodimeric construction; it is composed of a toxic A-chain possessing enzymatic action, and a receptor binding B-chain. Monoclonal antibodies were obtained with binding activities against either the A-chain or B-chain, and a surrogate non-toxic ricin analogue, TST10114, was determined to be suitable for characterization of the anti-ricin monoclonal antibodies. One potent anti-ricin A-chain neutralizing monoclonal antibody was chosen for chimerization, RAC18, which exhibited strong binding affinity and neutralizing properties. The constant regions of a human immunoglobulin G2 (IgG2) were used as the backbone for the recombinant chimeric antibody. The resulting chimeric RAC18-huG2 was transiently expressed in human-derived HEK 293F cells, purified, and assessed for binding characteristics and functional attributes.

Identiferoai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:MWU.1993/4526
Date12 April 2011
CreatorsVendramelli, Robert Matthew
ContributorsBerry, Jody (Medical microbiology), Corbett, Cindi (Medical Microbiology) Yao, Xiaojian (Medical Microbiology) Soussi-Gounni, Abdelilah (Immunology)
Source SetsLibrary and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada
Languageen_US
Detected LanguageEnglish

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