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• W87599195 abstract "Research Article1 October 1990free access The poliovirus receptor protein is produced both as membrane-bound and secreted forms. S. Koike S. Koike Department of Microbiology, Tokyo Metropolitan Institute of Medical Science, Japan. Search for more papers by this author H. Horie H. Horie Department of Microbiology, Tokyo Metropolitan Institute of Medical Science, Japan. Search for more papers by this author I. Ise I. Ise Department of Microbiology, Tokyo Metropolitan Institute of Medical Science, Japan. Search for more papers by this author A. Okitsu A. Okitsu Department of Microbiology, Tokyo Metropolitan Institute of Medical Science, Japan. Search for more papers by this author M. Yoshida M. Yoshida Department of Microbiology, Tokyo Metropolitan Institute of Medical Science, Japan. Search for more papers by this author N. Iizuka N. Iizuka Department of Microbiology, Tokyo Metropolitan Institute of Medical Science, Japan. Search for more papers by this author K. Takeuchi K. Takeuchi Department of Microbiology, Tokyo Metropolitan Institute of Medical Science, Japan. Search for more papers by this author T. Takegami T. Takegami Department of Microbiology, Tokyo Metropolitan Institute of Medical Science, Japan. Search for more papers by this author A. Nomoto A. Nomoto Department of Microbiology, Tokyo Metropolitan Institute of Medical Science, Japan. Search for more papers by this author S. Koike S. Koike Department of Microbiology, Tokyo Metropolitan Institute of Medical Science, Japan. Search for more papers by this author H. Horie H. Horie Department of Microbiology, Tokyo Metropolitan Institute of Medical Science, Japan. Search for more papers by this author I. Ise I. Ise Department of Microbiology, Tokyo Metropolitan Institute of Medical Science, Japan. Search for more papers by this author A. Okitsu A. Okitsu Department of Microbiology, Tokyo Metropolitan Institute of Medical Science, Japan. Search for more papers by this author M. Yoshida M. Yoshida Department of Microbiology, Tokyo Metropolitan Institute of Medical Science, Japan. Search for more papers by this author N. Iizuka N. Iizuka Department of Microbiology, Tokyo Metropolitan Institute of Medical Science, Japan. Search for more papers by this author K. Takeuchi K. Takeuchi Department of Microbiology, Tokyo Metropolitan Institute of Medical Science, Japan. Search for more papers by this author T. Takegami T. Takegami Department of Microbiology, Tokyo Metropolitan Institute of Medical Science, Japan. Search for more papers by this author A. Nomoto A. Nomoto Department of Microbiology, Tokyo Metropolitan Institute of Medical Science, Japan. Search for more papers by this author Author Information S. Koike1, H. Horie1, I. Ise1, A. Okitsu1, M. Yoshida1, N. Iizuka1, K. Takeuchi1, T. Takegami1 and A. Nomoto1 1Department of Microbiology, Tokyo Metropolitan Institute of Medical Science, Japan. The EMBO Journal (1990)9:3217-3224https://doi.org/10.1002/j.1460-2075.1990.tb07520.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Both genomic and complementary DNA clones encoding poliovirus receptors were isolated from genomic and complementary DNA libraries prepared from HeLa S3 cells, respectively. Nucleotide sequence analysis of these cloned DNAs revealed that the poliovirus receptor gene is approximately 20 kb long and contains seven introns in the coding region, and that at least four mRNA isoforms referring to the coding sequence are generated by alternative splicing and appear to encode four different molecules, that is, PVR alpha, PVR beta, PVR gamma and PVR delta. The predicted amino acid sequences indicate that PVR alpha and PVR delta, corresponding to the previously described cDNA clones H20A and H20B, respectively, are integral membrane proteins while the other two molecules described here for the first time lack a putative transmembrane domain. Mouse cell transformants carrying PVR alpha were permissive for poliovirus infection, but those carrying PVR beta were hardly permissive. In contrast to PVR alpha, PVR beta was not detected on the surface of the mouse cell transformants but was detected in the culture fluid by an immunological method using a monoclonal antibody against poliovirus receptor. Three types of splicing products for PVR alpha, PVR beta and PVR gamma were detected by polymerase chain reactions using appropriate primers in poly(A)+ RNAs of the brain, leukocyte, liver, lung and placenta of humans; the choice of primers used did not permit detection of PVR delta. In situ hybridization using a cDNA fragment as a probe demonstrated that the PVR gene is located at the band q13.1––13.2 of human chromosome 19. Previous ArticleNext Article Volume 9Issue 101 October 1990In this issue RelatedDetailsLoading ..." @default.
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• W87599195 title "The poliovirus receptor protein is produced both as membrane-bound and secreted forms." @default.
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