Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for its fusion activity.
Adv Exp Med Biol
; 342: 165-70, 1993.
Article
en En
| MEDLINE
| ID: mdl-8209724
ABSTRACT
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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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Glicoproteínas de Membrana
/
Procesamiento Proteico-Postraduccional
/
Proteínas del Envoltorio Viral
/
Virus de la Hepatitis Murina
/
Efecto Citopatogénico Viral
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Adv Exp Med Biol
Año:
1993
Tipo del documento:
Article