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High affinity anti-Internalin B VHH antibody fragments isolated f | 6880
Immunome Research

Immunome Research
Open Access

ISSN: 1745-7580

+44-20-4587-4809

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


2nd International Conference on Antibodies and Therapeutics

July 11-12, 2016 Philadelphia, USA

Mehdi Arbabi Ghahroudi

National Research Council Canada, Canada

Posters & Accepted Abstracts: Immunome Res

Abstract :

Development of rapid detection methodologies for food-borne and environmental pathogens is essential for safe-guarding the health of populations. Distribution of tainted foods and water can have a direct impact on human health, the food industry and consequently, on economies as a whole. Antibodies and antibody fragments have been historically used in detection platforms due to their antigen specificity and robust physicochemical properties. Camelid VHH fragments, also known as Nanobodies have desirable features such as high affinity, unique target specificities and high thermal stability and solubility, making them ideal detection reagents even under non-physiological conditions. We report, for the first time, the isolation and characterization of antibody fragments from the Camelidae heavy chain VHH libraries which bind with specificity and high affinity to the Listeria monocytogenes invasin, Internalin B (InlB). 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.

Biography :

Email: Mehdi.ArbabiGhahroudi@nrc-cnrc.gc.ca

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