Respiratory syncytial virus subunit vaccine based on a recombinant fusion protein expressed transiently in mammalian cells

Nallet, Sophie; Amacker, Mario; Westerfeld, Nicole; Baldi, Lucia; König, Iwo; Hacker, David L.; Zaborosch, Christiane; Zurbriggen, Rinaldo; Wurm, Florian Μ.

doi:10.1016/j.vaccine.2009.06.019

Cited by 18 publications

(13 citation statements)

References 25 publications

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“…The IRIV was composed of pure lipids, the RSV F protein and the influenza HA and NA proteins. This IRIV induced the production of neutralizing anti-F antibodies in BALB/c mice, but protection against RSV challenge and vaccine-enhanced immunopathology were not assessed [219]. NDV VLPs containing the NDV NP and M proteins and the ectodomains of the RSV F and G proteins fused to the NDV F and HN transmembrane and cytoplasmic domains, respectively, have been produced from transfected cells and shown to stimulate the production of neutralizing antibodies to both the F and G proteins in mice.…”

Section: Advances In Rsv Vaccine Developmentmentioning

confidence: 99%

Targeting RSV with Vaccines and Small Molecule Drugs

Costello¹,

Ray²,

Chaiwatpongsakorn³

et al. 2012

IDDT

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Respiratory syncytial virus (RSV) is the most significant cause of pediatric respiratory infections. Palivizumab (Synagis®), a humanized monoclonal antibody, has been used successfully for a number of years to prevent severe RSV disease in at-risk infants. However, despite intense efforts, there is no approved vaccine or small molecule drug for RSV. As an enveloped virus, RSV must fuse its envelope with the host cell membrane, which is accomplished through the actions of the fusion (F) glycoprotein, with attachment help from the G glycoprotein. Because of their integral role in initiation of infection and their accessibility outside the lipid bilayer, these proteins have been popular targets in the discovery and development of antiviral compounds and vaccines against RSV. This review examines advances in the development of antiviral compounds and vaccine candidates.

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Section: Advances In Rsv Vaccine Developmentmentioning

confidence: 99%

Targeting RSV with Vaccines and Small Molecule Drugs

Costello¹,

Ray²,

Chaiwatpongsakorn³

et al. 2012

IDDT

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show abstract

“…Particulate vaccines e.g. virus-like particles (VLPs), nanoparticles and virosomes have been used as new vaccine strategies to potentiate immune response against RSV antigens and have shown promising results [24–30]. A recent study using VLPs demonstrated that mice immunized with VLPs carrying RSV F or G protein had higher viral neutralizing antibodies in vitro and significantly decreased lung virus loads in vivo after live RSV challenge.…”

Section: Introductionmentioning

confidence: 99%

Nanoparticle Vaccines Encompassing the Respiratory Syncytial Virus (RSV) G Protein CX3C Chemokine Motif Induce Robust Immunity Protecting from Challenge and Disease

et al. 2013

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Nanoparticle vaccines were produced using layer-by-layer fabrication and incorporating respiratory syncytial virus (RSV) G protein polypeptides comprising the CX3C chemokine motif. BALB/c mice immunized with G protein nanoparticle vaccines produced a neutralizing antibody response that inhibited RSV replication in the lungs following RSV challenge. ELISPOT analysis showed that G nanoparticle vaccinated mice had increased levels of RSV G protein-specific IL-4 and IFN-γ secreting cells compared to controls following RSV challenge. Remarkably, RSV challenge of G protein nanoparticle vaccinated mice resulted in increased RSV M2-specific IL-4 and IFN-γ secreting T cells, and increased M2-specific H-2Kd-tetramer positive CD8+ T cells in the lungs compared to controls. Cell type analysis showed vaccination was not associated with increased pulmonary eosinophilia following RSV challenge. These results demonstrate that vaccination of mice with the RSV G protein nanoparticle vaccines induces a potent neutralizing antibody response, increased G protein- and M2- specific T cell responses, and a reduction in RSV disease pathogenesis.

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“…TGE may also be considered as an alternative method for the production of low‐dose proteins such as vaccines. [11,12] To this end, we have demonstrated the feasibility of large‐scale TGE for the production of the fusion protein from respiratory syncytial virus (RSV‐F) 11. Other candidate vaccines including human immunodeficiency virus 1 envelope glycoprotein and Rift Valley Fever virus‐like particles have been produced by PEI‐mediated TGE 12, 13.…”

Section: Introductionmentioning

confidence: 99%

Poly(ethyleneimine)‐Mediated Large‐Scale Transient Gene Expression: Influence of Molecular Weight, Polydispersity and N‐Propionyl Groups

Kadlecova

Nallet

Hacker

et al. 2012

Macromolecular Bioscience

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Three synthesis lots of linear poly(ethyleneimine) (PEI) are compared to a fully hydrolyzed linear PEI (commercially available as PEI "Max") regarding structure, polyplex formation with plasmid DNA, and transfection of suspension-adapted HEK-293E cells. PEI "Max" binds DNA more efficiently than the other PEIs, but it is the least effective in terms of transient recombinant protein yield. One PEI lot is fractionated by means of SEC. The fractions of high-M(n) PEI are the most efficient for complex formation and transfection. Nevertheless, the highest transient recombinant protein yields are achieved with unfractionated PEI. The results demonstrate that the polydispersity and charge density of linear PEI are important parameters for gene delivery to suspension-adapted HEK-293E cells.

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Respiratory syncytial virus subunit vaccine based on a recombinant fusion protein expressed transiently in mammalian cells

Cited by 18 publications

References 25 publications

Targeting RSV with Vaccines and Small Molecule Drugs

Targeting RSV with Vaccines and Small Molecule Drugs

Nanoparticle Vaccines Encompassing the Respiratory Syncytial Virus (RSV) G Protein CX3C Chemokine Motif Induce Robust Immunity Protecting from Challenge and Disease

Poly(ethyleneimine)‐Mediated Large‐Scale Transient Gene Expression: Influence of Molecular Weight, Polydispersity and N‐Propionyl Groups

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