Single-domain antibodies and their utility

From National Research Council Canada

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DOIResolve DOI: https://doi.org/10.1002/0471142735.im0217s103
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Name affiliation
  1. National Research Council of Canada. Human Health Therapeutics
  2. National Research Council of Canada
FormatText, Book chapter
Book titleCurrent Protocols in Immunology
ISBN9780471142737
IssueSUPPL 103
Article number2.17
Pages1–57
Subjectsingle-domain antibody; heavy-chain antibodies; VHH; antibody fragment; dimeric VHH; pentabodies; multivalency
Abstract
Engineered monoclonal antibody fragments have gained market attention due to their versatility and tailor-made potential and are now considered to be an important part of future immunobiotherapeutics. Single-domain antibodies (sdAbs), also known as nanobodies, are derived from VHHs [variable domains (V) of heavy-chain-only antibodies (HCAb)] of camelid heavy-chain antibodies. These nature-made sdAbs are well suited for various applications due to their favorable characteristics such as small size, ease of genetic manipulation, high affinity and solubility, overall stability, resistance to harsh conditions (e.g., low pH, high temperature), and low immunogenicity. Most importantly, sdAbs have the feature of penetrating into cavities and recognizing hidden epitopes normally inaccessible to conventional antibodies, mainly due to their protruding CDR3/H3 loops. In this unit, we will present and discuss comprehensive and step-by-step protocols routinely practiced in our laboratory for isolating sdAbs from immunized llamas (or other members of the Camelidae family) against target antigens using phage-display technology. Expression, purification, and characterization of the isolated sdAbs will then be described, followed by presentation of several examples of applications of sdAbs previously characterized in our laboratory and elsewhere.
Publication date
PublisherWiley
Wiley
LanguageEnglish
Peer reviewedYes
NPARC number23000612
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