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

J Immunol Methods

School of Environmental Sciences, University of Guelph, 50 Stone Road East, Guelph, ON, N1G 2W1, Canada; Department of Biology, Carleton University, Ottawa, ON, K1S 5B6, Canada; National Research Council Canada, Human Health Therapeutics-Biologics, 100 Sussex Drive, Ottawa, ON, K1A 0R6, Canada. Electronic address:

Published: January 2015

AI Article Synopsis

  • * Researchers isolated and characterized specific antibody fragments (VHH) from camelids that precisely bind to Internalin B, a protein associated with Listeria monocytogenes.
  • * This research is the first to report anti-InlB VHHs from camelids and shows that they do not cross-react with a similar protein, suggesting potential for new detection and medical technologies.

Article Abstract

The 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.

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http://dx.doi.org/10.1016/j.jim.2014.10.009DOI Listing

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