title: The infectivity of prM-containing partially mature West Nile virus does not require the activity of cellular furin-like proteases.
abstract: Cleavage of the flavivirus prM protein by a cellular furin-like protease is a hallmark of virion maturation. While this cleavage is a required step in the viral life cycle, it can be inefficient. Virions that retain uncleaved prM may be infectious. We investigated whether cleavage by furin of prM on partially mature West Nile virus (WNV) during virus entry contributes to infectivity. Using quantitative assays of WNV infection, we found that virions incorporating considerable amounts of uncleaved prM protein were insensitive to treatment of cells with a potent inhibitor of furin activity. Thus, partially mature WNV does not require furin-like proteases for infectivity.
authors: Viral Pathogenesis Section, Laboratory of Viral Diseases, National Institutes of Health, 33 North Drive, Building 33, Room 2E19A.2, Bethesda, MD 20892, USA.
authors: Swati
authors: S
authors: Mukherjee
authors: Tsai-Yu
authors: TY
authors: Lin
authors: Kimberly A
authors: KA
authors: Dowd
authors: Carolyn J
authors: CJ
authors: Manhart
authors: Theodore C
authors: TC
authors: Pierson
mesh_terms: D000818:Animals; D002460:Cell Line; D045683:Furin / Q000378:metabolism*; D006801:Humans; D011499:Protein Processing, Post-Translational; D014759:Viral Envelope Proteins / Q000378:metabolism*; D014902:West Nile virus / Q000254:growth & development / Q000502:physiology*
chemical_list: D014759:Viral Envelope Proteins; C074932:prM protein, Flavivirus; D045683:Furin