High affinity anti-Internalin B VHH antibody fragments isolated from naturally and artificially immunized repertoires

Alternative titleCharacterization of high affinity anti-Internalin B VHH antibody fragments isolated from naturally and artificially immunized repertoires
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DOIResolve DOI: http://doi.org/10.1016/j.jim.2014.10.009
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TypeArticle
Journal titleJournal of Immunological Methods
ISSN0022-1759
Volume416
Pages2939; # of pages: 11
SubjectListeria; Camelid; Single-domain antibody; Phage display; ELISA; Surface plasmon resonance
AbstractThe need for rapid and easy technologies for the detection of food-borne and environmental pathogens is essential for safeguarding the health of populations. Furthermore, distribution of tainted food and water can have consequences which can affect whole economies. Antibodies and antibody fragments have been historically used in detection platforms due to their antigen specificity and robust physicochemical properties. In this study, we report the isolation and characterization of antibody fragments from the heavy chain antibody repertoire (VHH) of Camelidae which bind with specificity and high affinity to the Listeria monocytogenes invasin, Internalin B (InlB). To the best of our knowledge, this is the first report of anti-InlB VHHs from camelids. These anti-InlB VHHs were not cross-reactive to the structurally related Listeria invasin Internalin A (InlA) and are potential reagents to be used in the development of detection and medical technologies.
Publication date
PublisherElsevier
LanguageEnglish
AffiliationHuman Health Therapeutics; National Research Council Canada
Peer reviewedYes
NRC numberNRC-HHT-53221
NPARC number21275314
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Record identifierf911f714-77af-4d0a-8db1-9a52916da470
Record created2015-06-05
Record modified2016-05-09
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