Incorporation of ORF2 from Porcine Circovirus Type 2(PCV2) into genetically encoded nanoparticles as a novel vaccine using a self-aggregating peptide

Zepeda–Cervantes, Jesús; Cruz-Reséndiz, Adolfo; Sampieri, Alicia; Carreón-Nápoles, Rosalba; Sánchez‐Betancourt, José Ivan; Vaca, Luis

doi:10.1016/j.vaccine.2019.02.044

Cited by 16 publications

(21 citation statements)

References 49 publications

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“…We developed a universal system to produce fusion proteins using as template the first 110 amino acids from AcMNPV polyhedrin protein. A transfer plasmid containing the strong polyhedrin promoter drives the expression of the PH followed by a poly-linker [29], which allows the insertion of any sequence to generate the fusion protein ( Fig. 1a).…”

Section: Resultsmentioning

confidence: 99%

“…Recently, this property has been used for biomedical purposes to incorporate antigens into particles for vaccine development [29]. However, the thermostability of the particles formed has not been characterized until now.…”

Section: Discussionmentioning

confidence: 99%

“…For this reason, the first step was to obtain a highly pure antigen easily and quickly. Because the PH GFP particles are insoluble in aqueous solutions, their purification is simple involving a one-step centrifugation process at low speed [28,29].…”

Section: Discussionmentioning

confidence: 99%

“…We have shown also that PH selfaggregates even when other proteins or peptides are fused to its sequence. Furthermore, we have recently shown that the ORF2 from porcine circovirus (PCV2) fused to PH injected in pigs results in the generation of neutralizing antibodies against circovirus [29]. However, no characterization of the particles formed or the thermostability of the vaccine and the adjuvant properties conferred by PH were analyzed in the aforementioned study [29].…”

Section: Introductionmentioning

confidence: 99%

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A self-aggregating peptide: implications for the development of thermostable vaccine candidates

et al. 2020

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Background: The use of biomaterials has been expanded to improve the characteristics of vaccines. Recently we have identified that the peptide PH (1-110) from polyhedrin self-aggregates and incorporates foreign proteins to form particles. We have proposed that this peptide can be used as an antigen carrying system for vaccines. However, the immune response generated by the antigen fused to the peptide has not been fully characterized. In addition, the adjuvant effect and thermostability of the particles has not been evaluated.Results: In the present study we demonstrate the use of a system developed to generate nano and microparticles carrying as a fusion protein peptides or proteins of interest to be used as vaccines. These particles are purified easily by centrifugation. Immunization of animals with the particles in the absence of adjuvant result in a robust and long-lasting immune response. Proteins contained inside the particles are maintained for over 1 year at ambient temperature, preserving their immunological properties. Conclusion:The rapid and efficient production of the particles in addition to the robust immune response they generate position this system as an excellent method for the rapid response against emerging diseases. The thermostability conferred by the particle system facilitates the distribution of the vaccines in developing countries or areas with no electricity.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A self-aggregating peptide: implications for the development of thermostable vaccine candidates

et al. 2020

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“…We have shown also that PH (1-110) self-aggregates even when other proteins or peptides are fused to its sequence. Furthermore, we have recently shown that the ORF2 from porcine circovirus (PCV2) fused to PH injected in pigs results in the generation of neutralizing antibodies against circovirus [29]. However, no characterization of the particles formed or the thermostability of the vaccine and the adjuvant properties conferred by PH were analyzed in the aforementioned study [29].…”

Section: Introductionmentioning

confidence: 99%

A self-aggregating peptide: Implications for the development of thermostable vaccine candidates

Cruz-Reséndiz¹,

Zepeda²,

Sampieri³

et al. 2019

Preprint

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Background: The use of biomaterials has been expanded to improve the characteristics of vaccines. Recently we have identified that the peptide PH(1-110) from polyhedrin self-aggregates and incorporates foreign proteins to form particles. We have proposed that this peptide can be used as an antigen carrying system for vaccines. However, the immune response generated by the antigen fused to the peptide has not been fully characterized. In addition, the adjuvant effect and thermostability of the particles has not been evaluated. Results: In the present study we demonstrate the use of a system developed to generate nano and microparticles carrying as a fusion protein peptides or proteins of interest to be used as vaccines. These particles are purified easily by centrifugation. Immunization of animals with the particles in the absence of adjuvant result in a robust and long-lasting immune response. Proteins contained inside the particles are maintained for over one year at ambient temperature, preserving their immunological properties. Conclusion: The rapid and efficient production of the particles in addition to the robust immune response they generate position this system as an excellent method for the rapid response against emerging diseases. The thermostability conferred by the particle system facilitates the distribution of the vaccines in developing countries or areas with no electricity.

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Multivalent display of chemical signals on self‐assembled peptide scaffolds

et al. 2021

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Self-assembled peptide materials have emerged as promising bioinspired tools for applications that include regenerative medicine, drug delivery, antimicrobial and vaccine development, optics, and catalysis. Peptide self-assembly mediated by noncovalent hydrogen bonding, coulombic, hydrophobic, and aromatic interactions gives rise to a variety of supramolecular structures that reflect on the nature of the constituent peptides. The emergent properties of these supramolecular peptide materials often depend on the multivalent presentation of functional appendages on the self-assembled scaffold. For example, the multivalent display of cell-signaling motifs on self-assembled peptide nanofibrils provides materials that are excellent extracellular matrix mimetics for tissue engineering applications. This review includes a discussion of chemical strategies that address the challenge of appending functional signal motifs in a multivalent display on self-assembled peptide and protein materials. In addition, recent examples of supramolecular peptide materials that rely on the multivalent display of chemical signals for the desired applications are presented. Collectively, this discussion illustrates the potential of self-assembled peptides as sustainable materials to address challenges in contemporary materials science and provides principles for the design of next-generation agents for a variety of applications.

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Incorporation of ORF2 from Porcine Circovirus Type 2(PCV2) into genetically encoded nanoparticles as a novel vaccine using a self-aggregating peptide

Cited by 16 publications

References 49 publications

A self-aggregating peptide: implications for the development of thermostable vaccine candidates

A self-aggregating peptide: implications for the development of thermostable vaccine candidates

A self-aggregating peptide: Implications for the development of thermostable vaccine candidates

Multivalent display of chemical signals on self‐assembled peptide scaffolds

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