ArticleProtein expression and purification2021
Novel expression of coat proteins from thermophilic bacteriophage ΦIN93 and evaluation for assembly into virus-like particles.
Article in Protein expression and purification, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed.
- Design, Co-Expression, and Evaluation for Assembly of the Structural Proteins from Thermophilic Bacteriophage ΦIN93.International journal of molecular sciences · 2025Article
- The Expanding Diversity of Viruses from Extreme Environments.International journal of molecular sciences · 2024Review
- Cell-penetrating peptides TAT and 8R functionalize P22 virus-like particles to enhance tissue distribution and retentionFrontiers in veterinary science · 2024Article
- Functional biology and biotechnology of thermophilic viruses.Essays in biochemistry · 2023Review
- Potential Applications of Thermophilic Bacteriophages in One Health.International journal of molecular sciences · 2023Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Virus-like particles (VLPs) have the potential to be used as display platforms to develop vaccines against infectious and non-infectious agents. However, most VLPs used as vaccine display platforms are derived from viruses that infect humans; unfortunately, most humans already have pre-existing antibodies against these platforms and thus, the immunogenicity of these vaccines may be compromised. VLP platforms derived from viruses that infect bacteria (bacteriophages), especially bacteriophages that infect bacteria, which do not colonize humans are less likely to have pre-existing antibodies against the platforms in the human population. In this study, we assessed whether two putative coat proteins (ORF13 and ORF14) derived from a thermophilic bacteriophage (ΦIN93) can be expressed and purified from a mesophilic bacterium such as E. coli. We also assessed whether expressed coat proteins can assemble to form VLPs. Truncated versions of ORF13 and ORF14 were successfully co-expressed in bacteria; the co-expressed truncated proteins formed oval structures that look like VLPs, but their sizes were less than those of an authentic ΦIN93 virus.
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Registered trials
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