The widespread but heterogeneous expression of the poliovirus receptor suggests that poliovirus tissue tropism is not solely due to receptor distribution and that the protein may have an endogenous function.
Heterogeneous expression beyond replication sites suggests tropism involves factors other than receptor distribution; leaves open endogenous receptor functions in human tissues.
Portions of the cellular receptor for poliovirus were expressed in Escherichia coli as fusion proteins with the product of the trpE gene. One of two antireceptor antisera obtained by immunizing rabbits with the fusion proteins blocked poliovirus infection. Western immunoblot analyses demonstrated that poliovirus receptor-related proteins were expressed in HeLa cells and a variety of human tissues, including those that are not sites of poliovirus replication. Tissue-specific variation in electrophoretic mobility, immunoreactivity, and subunit arrangement of poliovirus receptor-related proteins was observed. These results demonstrate that poliovirus tissue tropism cannot be explained by a limited distribution of receptor polypeptide, but may be the result of alternative splicing, posttranslational modifications, or both. In addition, the widespread but heterogeneous expression of the receptor suggests that the protein may have an important endogenous function.
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Freistadt et al. (1990) studied this question.
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