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Poliovirus can enter and infect mammalian cells by way of an intercellular adhesion molecule 1 pathway
H C Selinka1, A Zibert, E Wimmer
1Department of Microbiology, State University of New York, Stony Brook 11794.
Abstract:
Mouse fibroblast cell lines were transfected with truncated forms of the human poliovirus receptor (PVR) cDNA and tested for the expression of functional receptors for poliovirus. Several receptor constructs, all containing the coding region of the first 143 amino acids of PVR, were able to render mouse cells susceptible to poliovirus infection. A deletion of 65 amino acids in the first extracellular domain of PVR prevented virus attachment and infection. These data suggest that domain 1 is necessary and sufficient for the virus-receptor interaction. A PVR/intercellular adhesion molecule 1 hybrid receptor, expressing the PVR variable domain on a truncated receptor molecule for human rhinovirus 14, was shown to be a functional receptor for poliovirus. This observation indicates that, subsequent to attachment to the PVR-binding domain, poliovirus can use the same pathway as the major receptor group rhinoviruses to enter cells.
Insights
The first extracellular domain of the poliovirus receptor (PVR) is essential for poliovirus attachment and infection. This domain alone is sufficient to confer poliovirus susceptibility to mouse cells.
Area of Science:
- Virology
- Molecular Biology
- Cell Biology
Background:
- Poliovirus entry into host cells is mediated by the poliovirus receptor (PVR).
- Understanding the specific domains of PVR involved in virus binding is crucial for comprehending viral infection mechanisms.
Purpose of the Study:
- To identify the essential domains of the human poliovirus receptor (PVR) responsible for poliovirus binding and cell entry.
- To investigate whether PVR domain 1 is sufficient for mediating poliovirus infection.
Main Methods:
- Transfection of mouse fibroblast cell lines with truncated forms of human PVR cDNA.
- Testing for functional poliovirus receptor expression and susceptibility to poliovirus infection.
- Construction and testing of a PVR/intercellular adhesion molecule 1 hybrid receptor.
Main Results:
- Receptor constructs containing the first 143 amino acids of PVR rendered mouse cells susceptible to poliovirus infection.
- Deletion of 65 amino acids in the first extracellular domain abolished virus attachment and infection, indicating domain 1's necessity.
- A PVR/ICAM-1 hybrid receptor demonstrated functional poliovirus binding, suggesting shared entry pathways with rhinoviruses.
Conclusions:
- The first extracellular domain of PVR is both necessary and sufficient for poliovirus attachment and infection.
- Poliovirus may utilize similar cellular entry pathways as major group rhinoviruses after binding to the PVR-binding domain.