# Development of a novel and broadly applicable thermostable bacteriophage VLPs platforms for vaccine design, drug delivery, and imaging

> **NIH NIH R15** · MICHIGAN TECHNOLOGICAL UNIVERSITY · 2020 · $54,367

## Abstract

PROJECT SUMMARY
Virus-like particles (VLPs) resemble - in size, structure, and immunogenicity - the virus from which the coat or
envelope protein(s) are derived from except for the fact they lack a viral genome; VLPs are non-infectious and
are safe. These features have been exploited to develop VLP-based vaccines against human papillomaviruses
and hepatitis B virus; furthermore, coat proteins from ~70 viruses are currently being explored to develop VLP-
based vaccines against these viruses. VLPs from some of these viruses have also been used as display
platforms to develop chimeric VLPs displaying heterologous peptides from other infectious agents, tumor-
associated antigens and other metabolic diseases. The goal of these chimeric VLPs is to induce antibodies
against the heterologous antigen displayed on the platforms and not the platforms. In addition to serving as
display platforms, VLPs have also been used for targeted delivery of drugs or cargo to specific cancer cells.
While the candidate VLPs-based vaccines displaying heterologous peptides are very effective in animal
studies, in the majority of studies, VLPs platforms (including adenoviral VLPs or dodecahedron) are derived
from viruses that infect humans and in some cases, studies used VLPs platforms that had previously been
used to immunize the general population; a good example is HBV vaccine, with a global infant vaccination
coverage of 84% in 2015. Vaccines based on some of these platforms, with pre-existing antibodies in the
general population, are likely to be less immunogenic in humans. Additionally, there is a limitation on the size
of heterologous antigens that can be genetically displayed on some VLPs platforms making it challenging to
display a single peptide with multiple epitopes on the same VLPs. Moreover, most of the VLPs platforms are
temperature-sensitive making them less suitable in developing countries with poor refrigeration facilities.
In this proposal, the PI will develop and characterize novel thermostable bacteriophage VLPs platforms using
coat proteins from thermophilic viruses P23-77 and ΦIN93. P23-77 and ΦIN93 was isolated from bacteria that
grow at 70-75 °C. Thus VLPs derived from these viruses are likely to be stable at room temperature (RT) or
above RT. Additional benefit of these VLPs platforms is that because these viruses do not infect humans, the
human population lacks pre-existing neutralizing antibodies against the VLPs platforms; thus, the
immunogenicity of the platforms cannot be compromised by pre-existing antibodies. Also, many surface-
exposed loops on the capsid may tolerate larger insertions of heterologous antigens. The PI will co-express
three coat proteins from P23-77 and two coat proteins from ΦIN93. The PI will assess whether the coat
proteins can assemble into VLPs, if they VLPs are thermostable, can tolerate heterologous peptide insertions
from human papillomaviruses, and if VLPs are immunogenic in comparison to the virus(es).

## Key facts

- **NIH application ID:** 9880558
- **Project number:** 1R15AI146982-01A1
- **Recipient organization:** MICHIGAN TECHNOLOGICAL UNIVERSITY
- **Principal Investigator:** Ebenezer Tumban
- **Activity code:** R15 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2020
- **Award amount:** $54,367
- **Award type:** 1
- **Project period:** 2020-02-24 → 2020-09-30

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/9880558

## Citation

> US National Institutes of Health, RePORTER application 9880558, Development of a novel and broadly applicable thermostable bacteriophage VLPs platforms for vaccine design, drug delivery, and imaging (1R15AI146982-01A1). Retrieved via AI Analytics 2026-05-21 from https://api.ai-analytics.org/grant/nih/9880558. Licensed CC0.

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