Parvoviruses are small, non-enveloped viruses with a single-stranded DNA genome. They are known for their ability to infect a variety of hosts, including humans, animals, and insects. Virus-like particles (VLPs) are non-infectious mimics of viruses that lack the viral genetic material but retain the structural properties of the virus. VLPs are widely used in vaccine development and as tools for studying virus-host interactions.
Parvovirus VLPs are typically composed of the major capsid proteins VP1 and VP2. These proteins self-assemble into VLPs that resemble the native virus in structure and antigenicity. The VP1 protein contains unique regions that are crucial for the virus’s infectivity and immune recognition. Recombinant VLPs can be produced by expressing these capsid proteins in various expression systems, such as bacteria, yeast, insect cells, or mammalian cells .
The VP1 protein of parvoviruses plays a significant role in the virus’s life cycle. It contains a unique N-terminal region (VP1u) that is essential for the virus’s infectivity. This region undergoes conformational changes during infection, exposing specific epitopes that are recognized by the host immune system . The VP1 protein also contains phospholipase A2 (PLA2) activity, which is necessary for the virus to escape from the endosome and enter the host cell cytoplasm.
Recombinant VP1 VLPs are produced by expressing the VP1 protein in a suitable expression system. These VLPs can be used as vaccines or as tools for studying the immune response to parvovirus infections. The production of recombinant VP1 VLPs involves several steps, including cloning the VP1 gene, expressing the protein in a host cell, purifying the protein, and assembling it into VLPs. The resulting VLPs are structurally similar to the native virus and can elicit a strong immune response in the host .
Recombinant VP1 VLPs have several applications in research and medicine: