tetano
Editor, Senior Moderator
PLoS One. 2018 Apr 4;13(4):e0194830. doi: 10.1371/journal.pone.0194830. eCollection 2018.
[h=1]An immuno-assay to quantify influenza virus hemagglutinin with correctly folded stalk domains in vaccine preparations.[/h] Rajendran M[SUP]1,[/SUP][SUP]2[/SUP], Sun W[SUP]1[/SUP], Comella P[SUP]1,[/SUP][SUP]2[/SUP], Nachbagauer R[SUP]1[/SUP], Wohlbold TJ[SUP]1,[/SUP][SUP]2[/SUP], Amanat F[SUP]1[/SUP], Kirkpatrick E[SUP]1,[/SUP][SUP]2[/SUP], Palese P[SUP]1,[/SUP][SUP]3[/SUP], Krammer F[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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.
PMID: 29617394 DOI: 10.1371/journal.pone.0194830
Free full text
[h=1]An immuno-assay to quantify influenza virus hemagglutinin with correctly folded stalk domains in vaccine preparations.[/h] Rajendran M[SUP]1,[/SUP][SUP]2[/SUP], Sun W[SUP]1[/SUP], Comella P[SUP]1,[/SUP][SUP]2[/SUP], Nachbagauer R[SUP]1[/SUP], Wohlbold TJ[SUP]1,[/SUP][SUP]2[/SUP], Amanat F[SUP]1[/SUP], Kirkpatrick E[SUP]1,[/SUP][SUP]2[/SUP], Palese P[SUP]1,[/SUP][SUP]3[/SUP], Krammer F[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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.
PMID: 29617394 DOI: 10.1371/journal.pone.0194830
Free full text