Two domains that control prefusion stability and transport competence of the measles virus fusion protein.

ABSTRACT: Most viral glycoproteins mediating membrane fusion adopt a metastable native conformation and undergo major conformational changes during fusion. We previously described a panel of compounds that specifically prevent fusion induced by measles virus (MV), most likely by interfering with conformational rearrangements of the MV fusion (F) protein. To further elucidate the basis of inhibition and better understand the mechanism of MV glycoprotein-mediated fusion, we generated and characterized resistant MV variants. Spontaneous mutations conferring drug resistance were confirmed in transient assays and in the context of recombinant virions and were in all cases located in the fusion protein. Several mutations emerged independently at F position 462, which is located in the C-terminal heptad re

SUBMITTER: Doyle J 

PROVIDER: S-EPMC1346935 | biostudies-literature | 2006 Feb

REPOSITORIES: biostudies-literature