tetano
Editor, Senior Moderator
Antiviral Res. 2014 Aug 27. pii: S0166-3542(14)00245-9. doi: 10.1016/j.antiviral.2014.08.008. [Epub ahead of print]
Protection against influenza H7N9 virus challenge with a recombinant NP-M1-HSP60 protein vaccine construct in BALB/c mice.
Yang P1, Wang W2, Gu H3, Li Z4, Zhang K4, Wang Z4, Li R4, Duan Y3, Zhang S5, Wang X6.
Author information
Abstract
A novel influenza virus of H7N9 subtype circulated throughout China in 2013. The high fatality rate, appearance of several family clusters, and transmission in animal models observed during this outbreak accelerated efforts to identify effective strategies to prevent the spread of this influenza subtype. In this study, the recombinant protein NP-M1-HSP60, a fusion of the nucleoprotein and M1 matrix protein of the A/PR/8/34 (H1N1) influenza virus strain and HSP60, was effectively expressed in Escherichia coli and purified as a candidate component for an influenza vaccine. Intranasal immunization of female BALB/c mice with NP-M1-HSP60 in combination with an oil-in-water adjuvant twice at a 2-week interval induced robust humoral, mucosal, and cell-mediated immune responses. Moreover, this immunization strategy completely protected mice from lethal influenza H7N9 virus challenge and significantly inhibited viral replication in the challenged mouse lung. These data suggest that this vaccine construct has great potential for the basic development of an influenza H7N9 vaccine.
Copyright ? 2014 Elsevier B.V. All rights reserved.
KEYWORDS:
H7N9 vaccine; HSP60; Influenza A virus; M1 protein; Nucleoprotein
PMID:
25173575
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25173575
Protection against influenza H7N9 virus challenge with a recombinant NP-M1-HSP60 protein vaccine construct in BALB/c mice.
Yang P1, Wang W2, Gu H3, Li Z4, Zhang K4, Wang Z4, Li R4, Duan Y3, Zhang S5, Wang X6.
Author information
Abstract
A novel influenza virus of H7N9 subtype circulated throughout China in 2013. The high fatality rate, appearance of several family clusters, and transmission in animal models observed during this outbreak accelerated efforts to identify effective strategies to prevent the spread of this influenza subtype. In this study, the recombinant protein NP-M1-HSP60, a fusion of the nucleoprotein and M1 matrix protein of the A/PR/8/34 (H1N1) influenza virus strain and HSP60, was effectively expressed in Escherichia coli and purified as a candidate component for an influenza vaccine. Intranasal immunization of female BALB/c mice with NP-M1-HSP60 in combination with an oil-in-water adjuvant twice at a 2-week interval induced robust humoral, mucosal, and cell-mediated immune responses. Moreover, this immunization strategy completely protected mice from lethal influenza H7N9 virus challenge and significantly inhibited viral replication in the challenged mouse lung. These data suggest that this vaccine construct has great potential for the basic development of an influenza H7N9 vaccine.
Copyright ? 2014 Elsevier B.V. All rights reserved.
KEYWORDS:
H7N9 vaccine; HSP60; Influenza A virus; M1 protein; Nucleoprotein
PMID:
25173575
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25173575