title: High affinity anti-Internalin B VHH antibody fragments isolated from naturally and artificially immunized repertoires.
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.
authors.affiliation: School of Environmental Sciences, University of Guelph, 50 Stone Road East, Guelph, ON, N1G 2W1, Canada. Electronic address: robertwgene@gmail.com.
authors.forename: Robert W
authors.initials: RW
authors.lastname: Gene
authors.affiliation: School of Environmental Sciences, University of Guelph, 50 Stone Road East, Guelph, ON, N1G 2W1, Canada. Electronic address: Jyothi.Kumaran@nrc-cnrc.gc.ca.
authors.forename: Jyothi
authors.initials: J
authors.lastname: Kumaran
authors.affiliation: Department of Biochemistry, Faculty of Science, University of Ottawa, 75 Laurier Avenue East, Ottawa, ON, K1N 6N5, Canada. Electronic address: caroc074@uottawa.ca.
authors.forename: Cristina
authors.initials: C
authors.lastname: Aroche
authors.affiliation: National Research Council Canada, Human Health Therapeutics-Biologics, 100 Sussex Drive, Ottawa, ON, K1A 0R6, Canada. Electronic address: Henk.vanFaassen@nrc-cnrc.gc.ca.
authors.forename: Henk
authors.initials: H
authors.lastname: van Faassen
authors.affiliation: School of Environmental Sciences, University of Guelph, 50 Stone Road East, Guelph, ON, N1G 2W1, Canada. Electronic address: jchall@uoguelph.ca.
authors.forename: J Christopher
authors.initials: JC
authors.lastname: Hall
authors.affiliation: School of Environmental Sciences, University of Guelph, 50 Stone Road East, Guelph, ON, N1G 2W1, Canada; National Research Council Canada, Human Health Therapeutics-Biologics, 100 Sussex Drive, Ottawa, ON, K1A 0R6, Canada. Electronic address: Roger.MacKenzie@nrc-cnrc.gc.ca.
authors.forename: C Roger
authors.initials: CR
authors.lastname: MacKenzie
authors.affiliation: 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: Mehdi.ArbabiGhahroudi@nrc-cnrc.gc.ca.
authors.forename: Mehdi
authors.initials: M
authors.lastname: Arbabi-Ghahroudi
mesh_terms: D000818:Animals; D000906:Antibodies / Q000276:immunology*; D000918:Antibody Specificity / Q000276:immunology; D001426:Bacterial Proteins / Q000276:immunology*; D002161:Camelids, New World / Q000276:immunology; D003429:Cross Reactions / Q000276:immunology; D007114:Immunization / Q000379:methods; D007128:Immunoglobulin Fragments / Q000276:immunology*; D007143:Immunoglobulin Heavy Chains / Q000276:immunology; D008089:Listeria monocytogenes / Q000276:immunology; D008088:Listeriosis / Q000276:immunology; D008565:Membrane Proteins / Q000276:immunology*
chemical_list: D000906:Antibodies; D001426:Bacterial Proteins; D007128:Immunoglobulin Fragments; D007143:Immunoglobulin Heavy Chains; D008565:Membrane Proteins; C095768:inlB protein, Listeria monocytogenes
keywords: Camelid; ELISA; Listeria; Phage display; Single-domain antibody; Surface plasmon resonance