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An immuno-assay to quantify influenza virus hemagglutinin with correctly folded stalk domains in vaccine preparations.

PloS one (2018-04-05)
Madhusudan Rajendran, Weina Sun, Phillip Comella, Raffael Nachbagauer, Teddy John Wohlbold, Fatima Amanat, Ericka Kirkpatrick, Peter Palese, Florian Krammer
ABSTRACT

The standard method to quantify the hemagglutinin content of influenza virus vaccines is the single radial immunodiffusion assay. This assay primarily relies on polyclonal antibodies against the head domain of the influenza virus hemagglutinin, which is the main target antigen of influenza virus vaccines. Novel influenza virus vaccine candidates that redirect the immune response towards the evolutionary more conserved hemagglutinin stalk, including chimeric hemagglutinin and headless hemagglutinin constructs, are highly dependent on the structural integrity of the protein to present conformational epitopes for neutralizing antibodies. In this study, we describe a novel enzyme-linked immunosorbent assay that allows quantifying the amount of hemagglutinin with correctly folded stalk domains and which could be further developed into a potency assay for stalk-based influenza virus vaccines.

MATERIALS
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Product Description

Sigma-Aldrich
Anti-Human IgG (Fab specific)−Peroxidase antibody produced in goat, affinity isolated antibody