The NSm proteins of Rift Valley fever virus are dispensable for maturation, replication and infection

• Published in: Virology (New York, N.Y.) Vol. 359; no. 2; pp. 459 - 465
• Main Authors: Gerrard, Sonja R, Bird, Brian H, Albariño, Cesar G, Nichol, Stuart T
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 15-03-2007
• Subjects: Accessory proteins; Amino Acid Sequence; amino acid sequences; Animals; Base Sequence; Bunyaviridae; Bunyavirus; Cercopithecus aethiops; DNA, Complementary; Gene Deletion; Infectious Disease; Molecular Sequence Data; Mutation; Non-structural proteins; nucleotide sequences; Phlebovirus; Plasmid-based genetics; Rift Valley fever; Rift Valley fever virus; Rift Valley fever virus - genetics; Rift Valley fever virus - pathogenicity; Rift Valley fever virus - physiology; Vector-borne; Vero Cells; viral nonstructural proteins; viral proteins; Viral Proteins - metabolism; Virus Assembly - physiology; Virus replication; Virus Replication - physiology; Rift Valley fever virus; Plasmid-based genetics; Non-structural proteins; Accessory proteins; Bunyavirus; Virus replication; Phlebovirus; Vector-borne
• ISSN: 0042-6822; 1096-0341
• DOI: 10.1016/j.virol.2006.09.035

Abstract Rift Valley fever (RVF) virus belongs to the Bunyaviridae family of segmented negative-strand RNA viruses and causes mosquito-borne disease in sub-Saharan Africa. We report the development of a T7 RNA polymerase-driven plasmid-based genetic system for the virulent Egyptian isolate, ZH501. We have used this system to rescue a virus that has a 387 nucleotide deletion on the genomic M segment that eliminates the coding region for two non-structural proteins known as NSm. This virus, ΔNSm rZH501, is indistinguishable from the parental ZH501 strain with respect to expression of structural proteins and growth in cultured mammalian cells.