High avidity binding of engineered papaya mosaic virus virus-like particles to resting spores of Plasmodiophora Brassicae

Morin, Hélène; Tremblay, Marie-Hélène; Plante, Edith; Paré, Christine; Majeau, Nathalie; Hogue, Richard; Leclerc, Denis

doi:10.1016/j.jbiotec.2006.10.013

Cited by 10 publications

(8 citation statements)

References 19 publications

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“…However, we were able to isolate large amounts of the recombinant proteins harbouring fusions located after the residues 12 and 187 and, as expected, at the C-terminus (Figure 2AB). As observed by TEM, the three recombinant proteins (PapMV-HA11-12, PapMV-HA11-187 and PapMV-HA11-C) could self-assemble into nanoparticles that were similar in appearance to other recombinant nanoparticles reported previously by our group (Figure 2C) [3], [4], [5], [6], [7]. Dynamic light scattering (DLS) revealed that PapMV-HA11-12 and C yielded shorter VLPs with an average size of 67 nm and 66 nm, respectively (Figure 2D).…”

Section: Resultssupporting

confidence: 79%

“…Also, fusion of the universal M2e peptide antigen derived from influenza M2 protein was showed to trigger a protective humoral response against a lethal influenza infection in mice [3]. For each of those fusions and others [7], self-assembly of the recombinant PapMV CP into nanoparticles ranging from 60 to 100 nm in length was shown to be critical to the induction of an efficient humoral response to the fused peptide antigen [3], [4]. We have also shown that PapMV nanoparticles can trigger a cytotoxic (CTL) immune response to a fused CTL epitope through loading of MHC class I and the proliferation of CD8+ human T cells [6].…”

Section: Introductionmentioning

confidence: 99%

“…However, while the PapMV vaccine platform is clearly versatile, and has been shown to tolerate the fusion of several peptides to its C-terminus [3], [4], [5], [6], [7], it is also possible that the fusion of certain peptides could interfere with the assembly process of the protein into nanoparticles and consequently affect its ability to trigger a proper immune response. It is therefore of interest to search for other sites of fusion in the PapMV CP to improve this vaccine tool.…”

Section: Introductionmentioning

confidence: 99%

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Engineering of Papaya Mosaic Virus (PapMV) Nanoparticles through Fusion of the HA11 Peptide to Several Putative Surface-Exposed Sites

et al. 2012

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Papaya mosaic virus has been shown to be an efficient adjuvant and vaccine platform in the design and improvement of innovative flu vaccines. So far, all fusions based on the PapMV platform have been located at the C-terminus of the PapMV coat protein. Considering that some epitopes might interfere with the self-assembly of PapMV CP when fused at the C-terminus, we evaluated other possible sites of fusion using the influenza HA11 peptide antigen. Two out of the six new fusion sites tested led to the production of recombinant proteins capable of self assembly into PapMV nanoparticles; the two functional sites are located after amino acids 12 and 187. Immunoprecipitation of each of the successful fusions demonstrated that the HA11 epitope was located at the surface of the nanoparticles. The stability and immunogenicity of the PapMV-HA11 nanoparticles were evaluated, and we could show that there is a direct correlation between the stability of the nanoparticles at 37°C (mammalian body temperature) and the ability of the nanoparticles to trigger an efficient immune response directed towards the HA11 epitope. This strong correlation between nanoparticle stability and immunogenicity in animals suggests that the stability of any nanoparticle harbouring the fusion of a new peptide should be an important criterion in the design of a new vaccine.

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Section: Resultssupporting

confidence: 79%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Engineering of Papaya Mosaic Virus (PapMV) Nanoparticles through Fusion of the HA11 Peptide to Several Putative Surface-Exposed Sites

et al. 2012

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“…The use of VLPs for efficient presentation of epitopes foreign to the immune system [21, 35–37] on their surface can resolve the problem of bio-safety as relates to vaccine protein production. Today, special attention is paid to the construction of vector systems that express capsid proteins forming VLPs free of any RNA impurities.…”

Section: Introductionmentioning

confidence: 99%

New Viral Vector for Superproduction of Epitopes of Vaccine Proteins in Plants

et al. 2011

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The novel viral vectors PVX-CP AltMV and PVXdt-CP AltMV are superexpressors of the capsid protein (CP). These viral vectors were constructed on the basis of the potato virus X (PVX) genome andAlternantheramosaic virus (AltMV) CP gene. The expression, based on the hybrid viral vectors, is genetically safe, since the systemic transport and formation of infective viral particles are blocked. CP AltMV can self-assemble into virus-like particles (VLPs) in the absence of genomic RNA. The vectors can be used for the presentation of foreign peptides (including epitopes of human pathogens) on the surface of the VLP. The N-terminal extracellular domain (M2e) of the influenza virus A M2 protein and its truncated variant (ΔM2e) were used as model heterologous peptides for the construction of the chimeric CP AltMV. Chimeric CP AltMV retains its ability to self-assemble into VLP. The epitopes of the M2 influenza virus protein were not eliminated during the process of accumulation, polymerization and purification of chimeric VLP AltMV, providing evidence of the stability of chimeric VLP with C-terminal heterologous epitopes. It appears that VLP produced by the vectors PVX-CP AltMV and PVXdt-CP AltMV can be used in the field of biotechnology for the presentation of the epitopes of vaccine proteins on their surfaces. The chimeric VLP AltMV with the presented foreign epitopes can be used as candidate vaccines.

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“…Recently, engineered fluorescent Papaya mosaic virus (PapMV) virus-like particles (VLPs) were shown to bind to P. brassicae resting spores at least as efficiently as polyclonal antibodies. The PapMV VLPs are easily produced in high yields; hence, they could possibly form a basis for a new type of detection method (19).…”

mentioning

confidence: 99%

In Planta Quantification of Plasmodiophora brassicae Using Signature Fatty Acids and Real-Time PCR

et al. 2010

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Until now, molecular and biochemical methods have only been used to show whether or not Plasmodiophora brassicae is present in plant or soil samples but not to what extent. Here, in planta quantification of P. brassicae by whole-cell fatty acid (WCFA) measurements and real-time polymerase chain reaction (PCR) was evaluated. Arachidonic acid (ARA, 20:4) was the most abundant fatty acid in resting spores and was only found in infected roots, which indicates a potential of ARA as a biomarker for P. brassicae. A real-time PCR assay was developed using primers designed from the internal transcribed spacer region of the ribosomal DNA. Using these primers, it was possible to detect P. brassicae in infected roots 10 days after germination of plants sown in infested soil. A bioassay showed that the amounts of ARA found by WCFA analysis and the DNA found by real-time PCR in infected plants were well correlated. These measurements also correlated with the soil spore content and the assessed disease incidence and disease severity scores. Therefore, we conclude that WCFA analysis and real-time PCR are good tools for P. brassicae quantification that can be applied to basic studies of the pathogen and in resistance screens.

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High avidity binding of engineered papaya mosaic virus virus-like particles to resting spores of Plasmodiophora Brassicae

Cited by 10 publications

References 19 publications

Engineering of Papaya Mosaic Virus (PapMV) Nanoparticles through Fusion of the HA11 Peptide to Several Putative Surface-Exposed Sites

Engineering of Papaya Mosaic Virus (PapMV) Nanoparticles through Fusion of the HA11 Peptide to Several Putative Surface-Exposed Sites

New Viral Vector for Superproduction of Epitopes of Vaccine Proteins in Plants

In Planta Quantification of Plasmodiophora brassicae Using Signature Fatty Acids and Real-Time PCR

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