Evaluation of HBs, HBc, and frCP Virus-Like Particles for Expression of Human Papillomavirus 16 E7 Oncoprotein Epitopes

Pumpens, Paul; Ražanskas, Raimundas; Pushko, Peter; Renhof, Regina; Gusars, I.; Skrastiņa, Dace; Ose, Velta; Borisova, Galina; Sominskaya, Irina; Petrovskis, Ivars; Jansons, Juris; Sasnauskas, Kęstutis

doi:10.1159/000050084

Cited by 36 publications

(11 citation statements)

References 37 publications

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“…The ability to fuse to both ends of the AP205 VLP-subunit allows better display of N-or C- terminal epitopes which is often difficult for other VLPs. Indeed, VLPs such as those derived from the Hepatitis B core antigen (HBcAg), the bacteriophage fr or filamentous phage particles only allow fusion at one terminus of the subunit [37], [38]. The availability of VLPs suitable for fusing epitopes at either end is important, since for a number of epitopes, the protective immune response raised, is specific for their N- or C-terminal part (unpublished and [21]).…”

Section: Discussionmentioning

confidence: 99%

Versatile Virus-Like Particle Carrier for Epitope Based Vaccines

Tissot¹,

Renhofa

Schmitz³

et al. 2010

PLoS ONE

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173

119

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BackgroundRecombinant proteins and in particular single domains or peptides are often poorly immunogenic unless conjugated to a carrier protein. Virus-like-particles are a very efficient means to confer high immunogenicity to antigens. We report here the development of virus-like-particles (VLPs) derived from the RNA bacteriophage AP205 for epitope-based vaccines.Methodology/Principal FindingsPeptides of angiotensin II, S.typhi outer membrane protein (D2), CXCR4 receptor, HIV1 Nef, gonadotropin releasing hormone (GnRH), Influenza A M2-protein were fused to either N- or C-terminus of AP205 coat protein. The A205-peptide fusions assembled into VLPs, and peptides displayed on the VLP were highly immunogenic in mice. GnRH fused to the C-terminus of AP205 induced a strong antibody response that inhibited GnRH function in vivo. Exposure of the M2-protein peptide at the N-terminus of AP205 resulted in a strong M2-specific antibody response upon immunization, protecting 100% of mice from a lethal influenza infection.Conclusions/SignificanceAP205 VLPs are therefore a very efficient and new vaccine system, suitable for complex and long epitopes, of up to at least 55 amino acid residues in length. AP205 VLPs confer a high immunogenicity to displayed epitopes, as shown by inhibition of endogenous GnRH and protective immunity against influenza infection.

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Section: Discussionmentioning

confidence: 99%

Versatile Virus-Like Particle Carrier for Epitope Based Vaccines

Tissot¹,

Renhofa

Schmitz³

et al. 2010

PLoS ONE

Self Cite

173

119

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“…Protection appears to be provided by the neutralization of antibodies, from which titers can be improved by using aluminum-based salt adjuvants (9). Other platforms, such as the bacteriophage Q␤ (23), hepatitis B virus (HBV) VLPs made of viral core protein (25,30), parvovirus VLPs (1,27), and plant virus VLPs (5), have the capacity to carry epitopes and evoke strong antibody responses. HBV VLPs supplemented with CpG (33) and parvovirus VLPs (21) have also shown their capacity to induce CTL responses.…”

mentioning

confidence: 99%

Proteasome-Independent Major Histocompatibility Complex Class I Cross-Presentation Mediated by Papaya Mosaic Virus-Like Particles Leads to Expansion of Specific Human T Cells

Leclerc

Beauseigle

Denis

et al. 2007

J Virol

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The development of versatile vaccine platforms is a priority that is recognized by health authorities worldwide; such platforms should induce both arms of the immune system, the humoral and cytotoxic-Tlymphocyte responses. In this study, we have established that a vaccine platform based on the coat protein of papaya mosaic virus (PapMV CP), previously shown to induce a humoral response, can induce major histocompatibility complex (MHC) class I cross-presentation of HLA-A*0201 epitopes from gp100, a melanoma antigen, and from influenza virus M1 matrix protein. PapMV proteins were able to assemble into stable virus-like particles (VLPs) in a crystalline and repetitive structure. When we pulsed HLA-A*0201؉ antigenpresenting cells (APCs) with the recombinant PapMV FLU or gp100, we noted that antigen-specific CD8 ؉ T cells were highly reactive to these APCs, demonstrating that the epitope from the VLPs were processed and loaded on the MHC class I complex. APCs were preincubated with two different proteasome inhibitors, which did not affect the efficiency of peptide presentation on MHC class I. Classical presentation from an endogenous antigen was abolished in the same conditions. Clearly, antigen presentation mediated by the PapMV system was proteasome independent. Finally, PapMV-pulsed APCs had the capacity to expand highly avid antigenspecific T cells against the influenza virus M1 HLA-A*0201 epitope when cocultured with autologous peripheral blood mononuclear cells. This study demonstrates the potential of PapMV for MHC class I crosspresentation and for the expansion of human antigen-specific T cells. It makes VLPs from PapMV CP a very attractive platform to trigger cellular responses for vaccine development against chronic infectious diseases and cancers.

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“…Hepatitis B virus surface antigen VLPs tolerated insertion of an HPV E7 epitope (19 amino acids) and the hepatitis E antigen (56 amino acids) (Pumpens et al . ; Li et al . ).…”

Section: Yeast‐derived Vlps As Delivery Systems For Antigens Nucleicmentioning

confidence: 96%

“…The former approach has been used for VLPs from HBV, hamster polyomavirus and enterovirus 71 (Pumpens et al . ; Li et al . ; Mazeike et al .…”

Section: Yeast‐derived Vlps As Delivery Systems For Antigens Nucleicmentioning

confidence: 99%

Yeast as an expression system for producing virus-like particles: what factors do we need to consider?

Kim

2016

Lett Appl Microbiol

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The development of various types of virus-like particles (VLPs) has accelerated over the past two decades as the importance of VLPs for generating nextgeneration vaccines has been appreciated. Yeast has advantages such as scalable fermentation, low risk of contamination by adventitious agents, low production costs and the ability to produce VLPs with reliable qualities. It is generally recognized that yeast is suitable for producing VLPs that have simple structures and are produced intracellularly. However, recently there has been much effort to extend its applicability, and there is now evidence that it can be used as an expression platform for the productions of VLPs not only of nonenveloped viruses but also of enveloped viruses. Moreover, evidences indicated that yeast allows secretory VLP productions. Meanwhile, it has become evident that the quality and quantity of yeast-derived VLPs are influenced by the choice of plasmid and promoter, the ratio of the structural proteins produced. Here, we review the characteristics of the yeast expression system in terms of the production of VLP and compare it with other expression systems. We also consider strategies for VLP production in yeast and factors that need to be taken into account.

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Evaluation of HBs, HBc, and frCP Virus-Like Particles for Expression of Human Papillomavirus 16 E7 Oncoprotein Epitopes

Cited by 36 publications

References 37 publications

Versatile Virus-Like Particle Carrier for Epitope Based Vaccines

Versatile Virus-Like Particle Carrier for Epitope Based Vaccines

Proteasome-Independent Major Histocompatibility Complex Class I Cross-Presentation Mediated by Papaya Mosaic Virus-Like Particles Leads to Expansion of Specific Human T Cells

Yeast as an expression system for producing virus-like particles: what factors do we need to consider?

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