Expression of influenza A virus-derived peptides on a rotavirus VP6-based delivery platform
- PDF / 1,773,233 Bytes
- 5 Pages / 595.276 x 790.866 pts Page_size
- 9 Downloads / 134 Views
BRIEF REPORT
Expression of influenza A virus‑derived peptides on a rotavirus VP6‑based delivery platform Stina Gröhn1 · Suvi Heinimäki1 · Kirsi Tamminen1 · Vesna Blazevic1 Received: 13 June 2020 / Accepted: 9 September 2020 © The Author(s) 2020
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. Modern bioengineering technologies have facilitated the design of subunit vaccines as safe and affordable alternatives to conventional vaccines [1]. At the frontline of the new alternatives are self-assembling protein-derived nanoparticles, which can also be employed as platforms or nanocarriers. These particles can be decorated with heterologous antigens, including peptides, protein domains, or (poly) saccharides with significant biological relevance but poor immunogenicity on their own due to small size, incorrect configuration, or lack of stability [1]. A protein functioning as a carrier typically has a highly ordered particulate structure and a size that is optimal for uptake by antigenpresenting cells [2], efficiently inducing immune responses Handling Editor: Reimar Johne. Suvi Heinimäki, Kirsi Tamminen have contributed equally to this work. * Stina Gröhn [email protected] Suvi Heinimäki [email protected] Kirsi Tamminen [email protected] Vesna Blazevic [email protected] 1
Faculty of Medicine and Health Technology, Vaccine Development and Immunology/Vaccine Research Center, Tampere University, Arvo Ylpön katu 34, FI‑33520 Tampere, Finland
against the heteroantigens presented on the platform. One of the most frequently used platform technologies is based on virus-like particles [3] that have been successfully decorated with antigens of various origins, such as hepatitis B virus [4] and influenza virus [5]. Another promising nanocarrier is based on the rotavirus (RV) medium-layer VP6 protein, which forms various nanostructures when exposed to different physiological conditions [6]. These nanostructures are extremely immunogenic and have been shown to possess adjuvant properties when co-administered with antigens in vitro and in vivo [7–10]. It has been demonstrated previously that inserting foreign sequences by genetic fusion to the surface loops or N-terminus (N-t) of VP6 does not affect the structure of the VP6 monomer, allowing the insertion of at least a 15-amino-acid (aa) peptide [11, 12]. In the present study, we aimed to evaluate the effect of insertions of different sizes on the expression of VP6
Data Loading...
