Association of poliovirus proteins with the endoplasmic reticulum.
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.
D003902:Detergents / Q000494:pharmacology; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006146:Guanidines / Q000494:pharmacology; D007425:Intracellular Membranes / Q000378:metabolism; D008970:Molecular Weight; D017955:Poliovirus / Q000378:metabolism*; D011485:Protein Binding / Q000187:drug effects; D012260:Ribonucleases; D014357:Trypsin; D014465:Ultrasonics; D014508:Urea / Q000494:pharmacology; D014764:Viral Proteins / Q000378:metabolism*; D014779:Virus Replication
D003902:Detergents; D006146:Guanidines; D014764:Viral Proteins; D014508:Urea; D012260:Ribonucleases; D014357:Trypsin