Virus-like particles (VLPs) are stable assemblies made from viral capsid proteins, that structurally resemble the parent virus but do not contain the viral genome. In the last two decades, a multitude of biomedical and chemical usages have been proposed for VLPs, which includes scaffolding for antigen display and vaccination; delivery of drugs, oligonucleotides and macromolecules to specific cellular locations; diagnostics; cancer therapy and industry-level catalysis. While there are still concerns regarding systematic usage of VLPs for therapeutic applications; the utilization of VLPs for vaccination has known widespread commercial acceptance. The repetitive antigenic surfaces of VLPs are usually more authentic mimics of the parent virus and trigger stronger immune responses compared to traditional protein-based subunit vaccines or killed/inactivated vaccines which may have compromised immunogenicity. On the other hand, the non-infectious nature of VLPs ensures safety during production and application.
The protein-based nature of VLPs, coupled with the ability of viral proteins to self-associate, offers a platform with molecular level control and precision of supramolecular assembly. VLPs are excellent tools for analyzing the mode of virus assembly from component proteins. These pathways can also be modified for encapsulation of foreign cargo in VLPs, which has found widespread usage in packaging of fluorescent molecules for imaging, and chemotherapeutic drugs and siRNAs for delivery to specific tissue types. VLPs, like their parent virus capsids, retain the capability of engaging cell surface receptors and disassembling under permissive cellular conditions, thus releasing payloads. The repeating protein moieties in VLPs have also been modified for targeting to specific tissue types. Recently, advances in high resolution structural analysis and structurally-guided VLP design has broadened the applications and enhanced the potency of VLPs. However, there are still lingering questions, such as developing methods for large-scale production and storage of VLPs, particularly enveloped VLPs, as well as the safety and efficacy of VLP-based therapeutics, which need to be addressed for broadening the biomedical usage of VLPs.
The editors encourage the submission of Original Research, Reviews, Mini-Reviews, Method papers, and others in the following (but not limited to) topics:
- Virus-like particles as delivery vehicles
- Virus-like particles for antigen display and vaccination
- Usage of VLPs in catalysis and nanotechnology
- Usage of VLPs in diagnostics and cancer therapy
- Challenges in production and purification of VLPs
- Biophysical properties, structure, and functionalization of VLPs
Virus-like particles (VLPs) are stable assemblies made from viral capsid proteins, that structurally resemble the parent virus but do not contain the viral genome. In the last two decades, a multitude of biomedical and chemical usages have been proposed for VLPs, which includes scaffolding for antigen display and vaccination; delivery of drugs, oligonucleotides and macromolecules to specific cellular locations; diagnostics; cancer therapy and industry-level catalysis. While there are still concerns regarding systematic usage of VLPs for therapeutic applications; the utilization of VLPs for vaccination has known widespread commercial acceptance. The repetitive antigenic surfaces of VLPs are usually more authentic mimics of the parent virus and trigger stronger immune responses compared to traditional protein-based subunit vaccines or killed/inactivated vaccines which may have compromised immunogenicity. On the other hand, the non-infectious nature of VLPs ensures safety during production and application.
The protein-based nature of VLPs, coupled with the ability of viral proteins to self-associate, offers a platform with molecular level control and precision of supramolecular assembly. VLPs are excellent tools for analyzing the mode of virus assembly from component proteins. These pathways can also be modified for encapsulation of foreign cargo in VLPs, which has found widespread usage in packaging of fluorescent molecules for imaging, and chemotherapeutic drugs and siRNAs for delivery to specific tissue types. VLPs, like their parent virus capsids, retain the capability of engaging cell surface receptors and disassembling under permissive cellular conditions, thus releasing payloads. The repeating protein moieties in VLPs have also been modified for targeting to specific tissue types. Recently, advances in high resolution structural analysis and structurally-guided VLP design has broadened the applications and enhanced the potency of VLPs. However, there are still lingering questions, such as developing methods for large-scale production and storage of VLPs, particularly enveloped VLPs, as well as the safety and efficacy of VLP-based therapeutics, which need to be addressed for broadening the biomedical usage of VLPs.
The editors encourage the submission of Original Research, Reviews, Mini-Reviews, Method papers, and others in the following (but not limited to) topics:
- Virus-like particles as delivery vehicles
- Virus-like particles for antigen display and vaccination
- Usage of VLPs in catalysis and nanotechnology
- Usage of VLPs in diagnostics and cancer therapy
- Challenges in production and purification of VLPs
- Biophysical properties, structure, and functionalization of VLPs