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An In vitro Model to Study Immune Responses of Human Peripheral Blood Mononuclear Cells to Human Respiratory Syncytial Virus Infection
Published on: December 10, 2013
Recombinant VP4 of human rhinovirus induces permeability in model membranes
Matthew P Davis1, Graham Bottley, Lucy P Beales
1Institute for Molecular and Cellular Biology, Faculty of Biological Sciences, The University of Leeds, Leeds LS2 9JT, United Kingdom.
Abstract:
In common with all nonenveloped viruses, the mechanism of picornavirus membrane penetration during cell entry is poorly understood. The small, myristylated capsid protein VP4 has been implicated in this process. Here we show that recombinant VP4 of human rhinovirus 16 has the ability to associate with and induce membrane permeability in otherwise intact liposomes. This provides further evidence that VP4 plays a key role in picornavirus cell entry.
Insights
Picornavirus entry into cells is unclear. Researchers found that the VP4 protein from human rhinovirus 16 can disrupt liposome membranes, suggesting VP4 is key to viral cell entry.
Area of Science:
- Virology
- Molecular Biology
- Cell Biology
Background:
- Picornaviruses are nonenveloped viruses.
- The mechanism of picornavirus membrane penetration during cell entry is not well understood.
- The capsid protein VP4 has been implicated in picornavirus cell entry.
Purpose of the Study:
- To investigate the role of picornavirus VP4 protein in membrane penetration.
- To provide evidence for VP4's function in viral cell entry.
Main Methods:
- Produced recombinant VP4 protein from human rhinovirus 16.
- Assayed the ability of VP4 to associate with and induce permeability in liposomes.
Main Results:
- Recombinant VP4 associated with liposomes.
- VP4 induced membrane permeability in intact liposomes.
Conclusions:
- VP4 plays a significant role in picornavirus membrane penetration.
- These findings support the hypothesis that VP4 is essential for picornavirus cell entry.
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