Peptide vaccine candidates against classical swine fever virus: T cell and neutralizing antibody responses of dendrimers displaying E2 and NS2–3 epitopes

Monsò, Marta; Tarradas, Joan; Torre, Beatriz G. de la; Sánchez‐Madrid, Francisco; Ganges, Llilianne; Andreu, David

doi:10.1002/psc.1292

Cited by 33 publications

(26 citation statements)

References 56 publications

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“…Unfortunately, the complex crude product obtained did not enable a good isolation of the target product with four copies of CP3 in a desirable amount and purity to be used in biological assays. The difficulties found could be related with steric effects and have previously been reported by others .…”

Section: Resultssupporting

confidence: 65%

Synthetic peptides derived from an N‐terminal domain of the E2 protein of GB virus C in the study of GBV‐C/HIV‐1 co‐infection

Fernández

Chan

Egido

et al. 2012

Journal of Peptide Science

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Synthetic peptides derived from GB virus C (GBV-C) have previously been studied in our group for the development of new systems capable of diagnosing diseases caused by this humanotropic virus. We also recently described specific peptide domains of the E2 envelop protein of GBV-C that have the capacity to interfere with the HIV-1 fusion peptide, produce a notable decrease in cellular membrane fusion, and perturb HIV-1 infectivity in a dose-dependent manner. The present work discloses the design and synthesis of both linear and cyclic branched peptides based on a previously reported N-terminal sequence of the GBV-C E2 protein. Immunoassays and cell-cell fusion assays were performed to evaluate their diagnostic value to detect anti-GBV-C antibodies in HIV-1 patients, as well as their putative anti-HIV-1 activity as entry inhibitors. Our results showed that chemical modifications of the selected E2(7-26) linear peptide to afford cyclic architecture do not result in an enhanced inhibition of gp41 HIV-1-mediated cell-cell fusion nor improved sensitivity in the detection of GBV-C antibodies in HIV-1 co-infected patients. Thus, the ELISA data reinforce the potential utility of linear versions of the E2(7-26) region for the development of new peptide-based immunosensor devices for the detection of anti-GBV-C antibodies in HIV-1 co-infected patients.

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Section: Resultssupporting

confidence: 65%

Synthetic peptides derived from an N‐terminal domain of the E2 protein of GB virus C in the study of GBV‐C/HIV‐1 co‐infection

Fernández

Chan

Egido

et al. 2012

Journal of Peptide Science

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“…Conversely, very recent reports have suggested the use of this fragment in combination with others in order to increase the protective efficacy [73], [74]. Other authors for instance, give attention to peptides covering amino acids 829 to 837 or 844 to 865 used under more immunogenic presentations [72], [73], [75]. Whether this fragment could be the most immunogenic or fully protective against CSFV will require challenge trials in which more experimental groups, fragment combinations and displaying strategies are considered.…”

Section: Discussionmentioning

confidence: 99%

Conformational and Thermal Stability Improvements for the Large-Scale Production of Yeast-Derived Rabbit Hemorrhagic Disease Virus-Like Particles as Multipurpose Vaccine

et al. 2013

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Recombinant virus-like particles (VLP) antigenically similar to rabbit hemorrhagic disease virus (RHDV) were recently expressed at high levels inside Pichia pastoris cells. Based on the potential of RHDV VLP as platform for diverse vaccination purposes we undertook the design, development and scale-up of a production process. Conformational and stability issues were addressed to improve process control and optimization. Analyses on the structure, morphology and antigenicity of these multimers were carried out at different pH values during cell disruption and purification by size-exclusion chromatography. Process steps and environmental stresses in which aggregation or conformational instability can be detected were included. These analyses revealed higher stability and recoveries of properly assembled high-purity capsids at acidic and neutral pH in phosphate buffer. The use of stabilizers during long-term storage in solution showed that sucrose, sorbitol, trehalose and glycerol acted as useful aggregation-reducing agents. The VLP emulsified in an oil-based adjuvant were subjected to accelerated thermal stress treatments. None to slight variations were detected in the stability of formulations and in the structure of recovered capsids. A comprehensive analysis on scale-up strategies was accomplished and a nine steps large-scale production process was established. VLP produced after chromatographic separation protected rabbits against a lethal challenge. The minimum protective dose was identified. Stabilized particles were ultimately assayed as carriers of a foreign viral epitope from another pathogen affecting a larger animal species. For that purpose, a linear protective B-cell epitope from Classical Swine Fever Virus (CSFV) E2 envelope protein was chemically coupled to RHDV VLP. Conjugates were able to present the E2 peptide fragment for immune recognition and significantly enhanced the peptide-specific antibody response in vaccinated pigs. Overall these results allowed establishing improved conditions regarding conformational stability and recovery of these multimers for their production at large-scale and potential use on different animal species or humans.

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“…All peptides were C‐terminal carboxamides of either a bishomopropargylglycine (Bpg) residue ( 2–4 ) providing the alkyne functionality required for CuAAC (Scheme A) or, in the case of 8 , a Cys residue supplying the thiol group for thiol‐ene ligation (Scheme B). In all MAP syntheses, flexibility‐enhancing spacer units incorporated at all branching points, a modification reported to improve synthetic product quality,8,18 were used. For 3 and 4 , the spacer was 8‐amino‐3,6‐dioxaoctanoic acid (O 2 Oc), whereas 6‐aminohexanoic acid (Ahx) was used for 8 .…”

Section: Resultsmentioning

confidence: 99%

Convergent Synthesis of Glycodendropeptides by Click Chemistry Approaches

et al. 2012

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Mannosylation facilitates the uptake of immunogenic peptides by antigen‐processing cells expressing mannose receptors at their surface. Mannose‐receptor interactions not only induce internalization but also trigger strong T‐cell stimulation, such as that of the dendritic cell‐specific intercellular ICAM‐3 grabbing non‐integrin (DC‐SIGN), a lectin that plays a key role in the immune response against different pathogens. We describe here two efficient synthetic strategies for structurally well‐defined mannose‐displaying glycodendropeptides with up to 16 peptide and 9 mannose copies. Our approaches integrate previously optimized synthetic methods for producing both peptide and glycan dendrimers, and make extensive use of CuI‐catalyzed Huisgen 1,3‐dipolar cycloaddition for both the building of the glycodendron moieties and their subsequent conjugation to the peptide components. These strategies are versatile and straightforward enabling full control of chemical structure as well as readily tunable valency.

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Peptide vaccine candidates against classical swine fever virus: T cell and neutralizing antibody responses of dendrimers displaying E2 and NS2–3 epitopes

Cited by 33 publications

References 56 publications

Synthetic peptides derived from an N‐terminal domain of the E2 protein of GB virus C in the study of GBV‐C/HIV‐1 co‐infection

Synthetic peptides derived from an N‐terminal domain of the E2 protein of GB virus C in the study of GBV‐C/HIV‐1 co‐infection

Conformational and Thermal Stability Improvements for the Large-Scale Production of Yeast-Derived Rabbit Hemorrhagic Disease Virus-Like Particles as Multipurpose Vaccine

Convergent Synthesis of Glycodendropeptides by Click Chemistry Approaches

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