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Coronaviruses pp 165-170 | Cite as

Proteolytic Cleavage of the Murine Coronavirus Surface Glycoprotein is not Required for Its Fusion Activity

  • Roland Stauber
  • Michael Pfleiderer
  • Stuart Siddell
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 342)

Summary

The surface glycoprotein (S) of the murine hepatitis coronavirus MHV normally undergoes proteolytic cleavage during transport to the cell surface. To determine whether the cleavage of the MHV-JHM S glycoprotein is required to activate its ability to fuse cellular membranes, the protease recognition sequence in a cDNA copy of the S gene was altered from Arg-Arg-Ala-Arg-Arg into Ser-Val-Ser-Gly-Gly by site directed mutagenesis. The mutated and wild type S genes were expressed by means of recombinant vaccinia viruses and it could be shown that the mutated S protein was not cleaved when it was expressed in mouse DBT cells, in contrast to the wild type S protein. Nevertheless, the non-cleaved S protein induced extensive syncytium formation in mouse DBT cells. These results clearly indicate that the non-cleaved form of the MHV S protein is able to mediate cell membrane fusion. Thus, proteolytic cleavage is not an absolute requirement for its fusion function.

Keywords

Syncytium Formation Fusion Activity Recombinant Vaccinia Virus Fusion Function General Virology 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1994

Authors and Affiliations

  • Roland Stauber
    • 1
  • Michael Pfleiderer
    • 1
  • Stuart Siddell
    • 1
  1. 1.Institut für VirologieUniversität WürzburgWürzburgGermany

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