TY - JOUR
T1 - An immuno-assay to quantify influenza virus hemagglutinin with correctly folded stalk domains in vaccine preparations
AU - Rajendran, Madhusudan
AU - Sun, Weina
AU - Comella, Phillip
AU - Nachbagauer, Raffael
AU - Wohlbold, Teddy John
AU - Amanat, Fatima
AU - Kirkpatrick, Ericka
AU - Palese, Peter
AU - Krammer, Florian
N1 - Publisher Copyright:
© 2018 Rajendran et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
PY - 2018/4
Y1 - 2018/4
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85044994495&partnerID=8YFLogxK
U2 - 10.1371/journal.pone.0194830
DO - 10.1371/journal.pone.0194830
M3 - Article
C2 - 29617394
AN - SCOPUS:85044994495
SN - 1932-6203
VL - 13
JO - PLoS ONE
JF - PLoS ONE
IS - 4
M1 - e0194830
ER -