tetano
Editor, Senior Moderator
Hum Vaccin Immunother. 2013 Jan 7;9(3). [Epub ahead of print]
A plant-produced H1N1 trimeric hemagglutinin protects mice from a lethal influenza virus challenge.
Shoji Y, Jones RM, Mett V, Chichester JA, Musiychuk K, Sun X, Tumpey TM, Green BJ, Shamloul M, Norikane J, Bi H, Hartman CE, Bottone C, Stewart M, Streatfield SJ, Yusibov V.
Source
Fraunhofer USA Center for Molecular Biotechnology; Newark, DE USA.
Abstract
The increased worldwide awareness of seasonal and pandemic influenza, including pandemic H1N1 virus, has stimulated interest in the development of economic platforms for rapid, large-scale production of safe and effective subunit vaccines. In recent years, plants have demonstrated their utility as such a platform and have been used to produce vaccine antigens against various infectious diseases. Previously, we have produced in our transient plant expression system a recombinant monomeric hemagglutinin (HA) protein (HAC1) derived from A/California/04/09 (H1N1) strain of influenza virus and demonstrated its immunogenicity and safety in animal models and human volunteers. In the current study, to mimic the authentic HA structure presented on the virus surface and to improve stability and immunogenicity of the HA antigen, we generated trimeric HA by introducing a trimerization motif from a heterologous protein into the HA sequence. Here, we describe the engineering, production in Nicotiana benthamiana plants, and characterization of the highly purified recombinant trimeric HA protein (tHA-BC) from A/California/04/09 (H1N1) strain of influenza virus. The results demonstrate the induction of serum hemagglutination inhibition antibodies by tHA-BC and its protective efficacy in mice against a lethal viral challenge, at levels comparable with the licensed egg-based H1N1 influenza vaccine. In addition, the immunogenic and protective doses of tHA-BC were much lower compared to monomeric HAC1. Further investigation into the optimum vaccine dose and/or regimen as well as the stability of trimerized HA is necessary to determine whether trimeric HA is a more potent vaccine antigen than monomeric HA.
PMID:
23296194
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/23296194
A plant-produced H1N1 trimeric hemagglutinin protects mice from a lethal influenza virus challenge.
Shoji Y, Jones RM, Mett V, Chichester JA, Musiychuk K, Sun X, Tumpey TM, Green BJ, Shamloul M, Norikane J, Bi H, Hartman CE, Bottone C, Stewart M, Streatfield SJ, Yusibov V.
Source
Fraunhofer USA Center for Molecular Biotechnology; Newark, DE USA.
Abstract
The increased worldwide awareness of seasonal and pandemic influenza, including pandemic H1N1 virus, has stimulated interest in the development of economic platforms for rapid, large-scale production of safe and effective subunit vaccines. In recent years, plants have demonstrated their utility as such a platform and have been used to produce vaccine antigens against various infectious diseases. Previously, we have produced in our transient plant expression system a recombinant monomeric hemagglutinin (HA) protein (HAC1) derived from A/California/04/09 (H1N1) strain of influenza virus and demonstrated its immunogenicity and safety in animal models and human volunteers. In the current study, to mimic the authentic HA structure presented on the virus surface and to improve stability and immunogenicity of the HA antigen, we generated trimeric HA by introducing a trimerization motif from a heterologous protein into the HA sequence. Here, we describe the engineering, production in Nicotiana benthamiana plants, and characterization of the highly purified recombinant trimeric HA protein (tHA-BC) from A/California/04/09 (H1N1) strain of influenza virus. The results demonstrate the induction of serum hemagglutination inhibition antibodies by tHA-BC and its protective efficacy in mice against a lethal viral challenge, at levels comparable with the licensed egg-based H1N1 influenza vaccine. In addition, the immunogenic and protective doses of tHA-BC were much lower compared to monomeric HAC1. Further investigation into the optimum vaccine dose and/or regimen as well as the stability of trimerized HA is necessary to determine whether trimeric HA is a more potent vaccine antigen than monomeric HA.
PMID:
23296194
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/23296194