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.
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Stauber, R., Pfleiderer, M., Siddell, S. (1994). Proteolytic Cleavage of the Murine Coronavirus Surface Glycoprotein is not Required for Its Fusion Activity. In: Laude, H., Vautherot, JF. (eds) Coronaviruses. Advances in Experimental Medicine and Biology, vol 342. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2996-5_26
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DOI: https://doi.org/10.1007/978-1-4615-2996-5_26
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