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.
Highlights
The traditional method to measure the potency of influenza virus vaccines is the single radial immunodiffusion (SRID) assay [1, 2]
This assay has been accepted by the United States Food and Drug Administration (FDA) since 1978 for the measurement of the hemagglutinin (HA) content of influenza vaccines based on antibodies to the HA globular head domain [3]
Development of a capture enzyme-linked immunosorbent assay (ELISA) to quantify HA with properly folded stalk domains We initially generated and characterized different murine monoclonal antibodies that bind to epitopes on the globular head domain of different HA subtypes
Summary
The traditional method to measure the potency of influenza virus vaccines is the single radial immunodiffusion (SRID) assay [1, 2]. This assay has been accepted by the United States Food and Drug Administration (FDA) since 1978 for the measurement of the hemagglutinin (HA) content of influenza vaccines based on antibodies to the HA globular head domain [3]. Influenza virus vaccine candidates that are based on inducing antibodies against the conserved stalk domain of the HA have been developed [8, 9]. The majority of neutralizing anti-stalk antibodies bind to conformational
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