tetano
Editor, Senior Moderator
Arch Virol
. 2020 Oct 16.
doi: 10.1007/s00705-020-04847-5. Online ahead of print.
Expression of influenza A virus-derived peptides on a rotavirus VP6-based delivery platform
Stina Gr?hn[SUP] 1 [/SUP], Suvi Heinim?ki[SUP] 2 [/SUP], Kirsi Tamminen[SUP] 2 [/SUP], Vesna Blazevic[SUP] 2 [/SUP]
Affiliations
Abstract
Recombinant protein technology enables the engineering of modern vaccines composed of a carrier protein displaying poorly immunogenic heterologous antigens. One promising carrier is based on the rotavirus inner-capsid VP6 protein. We explored different VP6 insertion sites for the presentation of two peptides (23 and 140 amino acids) derived from the M2 and HA genes of influenza A virus. Both termini and three surface loops of VP6 were successfully exploited as genetic fusion sites, as demonstrated by the expression of the fusion proteins. However, further studies are needed to assess the morphology and immunogenicity of these constructs.
. 2020 Oct 16.
doi: 10.1007/s00705-020-04847-5. Online ahead of print.
Expression of influenza A virus-derived peptides on a rotavirus VP6-based delivery platform
Stina Gr?hn[SUP] 1 [/SUP], Suvi Heinim?ki[SUP] 2 [/SUP], Kirsi Tamminen[SUP] 2 [/SUP], Vesna Blazevic[SUP] 2 [/SUP]
Affiliations
- PMID: 33067651
- DOI: 10.1007/s00705-020-04847-5
Abstract
Recombinant protein technology enables the engineering of modern vaccines composed of a carrier protein displaying poorly immunogenic heterologous antigens. One promising carrier is based on the rotavirus inner-capsid VP6 protein. We explored different VP6 insertion sites for the presentation of two peptides (23 and 140 amino acids) derived from the M2 and HA genes of influenza A virus. Both termini and three surface loops of VP6 were successfully exploited as genetic fusion sites, as demonstrated by the expression of the fusion proteins. However, further studies are needed to assess the morphology and immunogenicity of these constructs.