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Journal of Virology logoLink to Journal of Virology
. 1984 Dec;52(3):777–783. doi: 10.1128/jvi.52.3.777-783.1984

Association of poliovirus proteins with the endoplasmic reticulum.

D R Tershak
PMCID: PMC254596  PMID: 6092710

Abstract

Poliovirus proteins, except P3-7c, are associated with the endoplasmic reticulum after extraction of the cytoplasm and centrifugation of membranes to equilibrium in sucrose gradients. Proteins P3-2, P2-X, and P3-9 are found preferentially among the rough endoplasmic reticulum, whereas P3-7c is located in smooth endoplasmic reticulum fractions. P3-7c is probably not membrane associated, since it can be separated from membranes after centrifugation in buffer. However, P3-4a, P2-5b, P2-X, and P3-9 are avidly bound to membranes and cannot be dislodged with high-ionic-strength buffer containing EDTA or 4 M urea. These proteins are digested by trypsin, indicating peripheral rather than internal localization.

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Selected References

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