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Sequence and topology of a model intracellular membrane protein, E1 glycoprotein, from a coronavirus

Nature volume 308, pages 751–752 (1984)Cite this article

Abstract

In the eukaryotic cell, both secreted and plasma membrane proteins are synthesized at the endoplasmic reticulum, then transported, via the Golgi complex, to the cell surface1–4. Each of the compartments of this transport pathway carries out particular metabolic functions5–8, and therefore presumably contains a distinct complement of membrane proteins. Thus, mechanisms must exist for localizing such proteins to their respective destinations. However, a major obstacle to the study of such mechanisms is that the isolation and detailed analysis of such internal membrane proteins pose formidable technical problems. We have therefore used the E1 glycoprotein from coronavirus MHV-A59 as a viral model for this class of protein. Here we present the primary structure of the protein, determined by analysis of cDNA clones prepared from viral mRNA. In combination with a previous study of its assembly into the endoplasmic reticulum membrane9, the sequence reveals several unusual features of the protein which may be related to its intracellular localization.

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Author notes

  1. Sjef Smeekens

    Present address: Molecular Cell Biology Group, State University of Utrecht, 3509 CH, Utrecht, The Netherlands

  2. Heiner Niemann: Institut für Virologie, Fachbereich Humanmedizin der Justus-Liebig Universität, Giessen, FRG

  3. Sjef Smeekens and Peter Rottier: Institute of Virology, Veterinary Faculty, State University of Utrecht, 3509 TD Utrecht, The Netherlands

Authors and Affiliations

  1. European Molecular Biology Laboratory, Postfach 10.2209, 6900, Heidelberg, FRG

    John Armstrong, Heiner Niemann, Sjef Smeekens, Peter Rottier & Graham Warren

Authors
  1. John Armstrong
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  2. Heiner Niemann
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  4. Peter Rottier
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Armstrong, J., Niemann, H., Smeekens, S. et al. Sequence and topology of a model intracellular membrane protein, E1 glycoprotein, from a coronavirus. Nature 308, 751–752 (1984). https://doi.org/10.1038/308751a0

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