Biotechnological applications of occlusion bodies of Baculoviruses

López, María Gabriela; Diez, Michay; Alfonso, Victoria; Taboga, Oscar

doi:10.1007/s00253-018-9130-2

Cited by 16 publications

(11 citation statements)

References 60 publications

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“…The use of polyhedrin protein as a biotechnological tool has increased mainly due to the intrinsic capacity of selfaggregation [27]. In addition, we have shown that using only the first 110 amino acids of polyhedrin (PH ) retains the self-aggregation property [28].…”

Section: Discussionmentioning

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: Discussionmentioning

confidence: 99%

“…One of the most studied insect viruses that forms polyhedra is the Autographa californica multiple nucleopolyhedrovirus (AcMNPV) [26,27].…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2020

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“…The use of polyhedrin protein as a biotechnological tool has increased mainly due to the intrinsic capacity of self-aggregation [27]. In addition, we have shown that using only the first 110 amino acids of polyhedrin (PH (1-110) ) retains the self-aggregation property [30].…”

Section: Discussionmentioning

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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“…Transfer vectors were obtained by cloning esat-6, cfp-10, and Rv3615c genes in NotI and SpeI restriction sites in the multiple cloning site of vector pFBDPOLH/POLH [López et al, 2018a]. The correct insertion of each gene in the final transfer vectors was confirmed by restriction enzymes and sequencing.…”

Section: Expression and Purification Of Polh-esat-6 Polh-cfp-10 Andmentioning

confidence: 99%

“…As an alternative, foreign genes can also be expressed as a fusion protein to polyhedrin. The advantage of this strategy is that the polyhedrin moiety in the fusion protein drives the localization of a heterologous antigen to an insoluble, crystalline protein matrix called polyhedron or occlusion body (OB), which facilitates the protein purification pro- cedures [López et al, 2018a]. Additionally, baculoviruses do not infect vertebrates and therefore no humoral or cellular immune responses would occur in vertebrates against baculovirus proteins.…”

Section: Introductionmentioning

confidence: 99%

Production of <b><i>Mycobacterium bovis</i></b> Antigens Included in Recombinant Occlusion Bodies of Baculovirus

et al. 2019

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Bovine tuberculosis (bTB) is a disease produced by Mycobacterium bovis that affects livestock, wild animals, and humans. The classical diagnostic method to detect bTB is measuring the response induced with the intradermal injection of purified protein derivative of M. bovis (PPDb). Another ancillary bTB test detects IFN-γ produced in whole blood upon stimulation with PPDb, protein/peptide cocktails, or individual antigens. Among the most used M. bovis antigens in IFN-γ assays are the secreted proteins ESAT-6 and CFP-10, which together with antigen Rv3615c improve the sensitivity of the test in comparison to PPDb. Protein reagents for immune stimulation are generally obtained from Escherichia coli, because this bacterium produces a high level of recombinant proteins. However, E. coli recombinant antigens are in general contaminated with lipopolysaccharides and other components that produce non-specific IFN-γ secretion in in vitro assays. In this work, we produced the relevant ESAT-6, CFP-10, and Rv3615c M. bovis antigens as fusions to the polyhedrin protein from the baculovirus AcMNPV. We obtained chimeric proteins effectively incorporated to the occlusion bodies and easily purified the recombinant polyhedra with no reactive contaminants. In an IFN-γ assay, these fusion proteins showed equivalent sensibility but better specificity than the same M. bovis proteins produced in E. coli.

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Biotechnological applications of occlusion bodies of Baculoviruses

Cited by 16 publications

References 60 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

Production of <b><i>Mycobacterium bovis</i></b> Antigens Included in Recombinant Occlusion Bodies of Baculovirus

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