Isolation and characterization of clostridium difficile toxin-specific single-domain antibodies

  1. Get@NRC: Isolation and characterization of clostridium difficile toxin-specific single-domain antibodies (Opens in a new window)
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Journal titleMethods in Molecular Biology
Pages211239; # of pages: 29
SubjectClostridium difficile toxin A; Clostridium difficile toxin B; epitope; nanobody; recombinant antibody; bacterial toxin; epitope; immunoglobulin G; immunoglobulin heavy chain; immunoglobulin M; animal experiment; antibody affinity; antibody production; antibody specificity; article; binding affinity; camel; Clostridium difficile; complementarity determining region; human; immunization; male; molecular weight; nonhuman; priority journal; animal; Artiodactyla; blood; cell surface display; immunology; isolation and purification; peptide library; Animals; Antibody Affinity; Antibody Specificity; Bacterial Toxins; Camelids, New World; Cell Surface Display Techniques; Clostridium difficile; Epitopes; Immunoglobulin G; Immunoglobulin Heavy Chains; Immunoglobulin M; Male; Peptide Library; Single-Domain Antibodies
AbstractCamelidae single-domain antibodies (VHHs) are a unique class of small binding proteins that are promising inhibitors of targets relevant to infection and immunity. With VHH selection from hyperimmunized phage display libraries now routine and the fact that VHHs possess long, extended complementarity- determining region (CDR3) loop structures that can access traditionally immunosilent epitopes, VHH-based inhibition of targets such as bacterial toxins are being explored. Toxin A and toxin B are high molecular weight exotoxins (308 kDa and 269 kDa, respectively) secreted by Clostridium difficile that are the causative agents of C. difficile-associated diseases in humans and in animals. Here, we provide protocols for the rapid generation of C. difficile toxin A-and toxin B-specific VHHs by llama immunization and recombinant antibody/phage display technology approaches and for further characterization of the VHHs with respect to toxin-binding affinity and specificity and the conformational nature of their epitopes. © 2012 Springer Science+Business Media, LLC.
Publication date
AffiliationNational Research Council Canada (NRC-CNRC); NRC Institute for Biological Sciences (IBS-ISB)
Peer reviewedYes
NPARC number21269183
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Record identifier2cfdb556-99b4-40c8-8adc-f847c3b640f7
Record created2013-12-12
Record modified2016-05-09
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