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Palmitoylation of Semliki Forest virus glycoproteins in insect cells (C 6/36) occurs in an early compartment and is coupled to the cleavage of the precursor p 62

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Summary

The acylation of the envelope proteins of Semliki Forest virus by palmitic acid in infected mosquito (C 6/36) cells was investigated. It is shown that in these cells palmitic acid was incorporated post-translationally via hydroxylamine-labile linkages onto cysteines in the inner domains of the viral envelope proteins. The kinetics of incorporation, however, differed considerably as compared to higher eukaryotic cells. (i) The precursor of the envelope proteins E2 and E3, p 62, was weakly and incompletely palmitoylated irrespective of the duration of labeling. (ii) Under all conditions tested complete acylation of E2 was delayed as compared to E1. (iii) Heavy protein complexes were formed consisting of unacylated p 62 and partially unacylated E1. From this data, we conclude that during the maturation of SFV glycoproteins in mosquito cells differently acylated intermediates of p 62/E2 exist. Furthermore, acylation of p 62/E2 and cleavage of p 62 are coupled events, occurring in an early compartment and allowing the release of the envelope oligomers for transport.

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  1. H. Y. Naim

    Present address: Southwestern Medical Center, Department of Biochemistry, The University of Texas at Dallas, Dallas, TX, USA

Authors and Affiliations

  1. Institute of Medical Microbiology, University of Berne, Berne, Switzerland

    C. G. Schärer, H. Y. Naim & H. Koblet

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  3. H. Koblet
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Schärer, C.G., Naim, H.Y. & Koblet, H. Palmitoylation of Semliki Forest virus glycoproteins in insect cells (C 6/36) occurs in an early compartment and is coupled to the cleavage of the precursor p 62. Archives of Virology 132, 237–254 (1993). https://doi.org/10.1007/BF01309536

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  • DOI: https://doi.org/10.1007/BF01309536

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