Characterization of the Golgi Retention Motif of Rift Valley Fever Virus GN Glycoprotein

AUTOR(ES)

Gerrard, Sonja R.

FONTE

American Society for Microbiology

RESUMO

As Rift Valley fever (RVF) virus, and probably all members of the family Bunyaviridae, matures in the Golgi apparatus, the targeting of the virus glycoproteins to the Golgi apparatus plays a pivotal role in the virus replication cycle. No consensus Golgi localization motif appears to be shared among the glycoproteins of these viruses. The viruses of the family Bunyaviridae synthesize their glycoproteins, GN and GC, as a polyprotein. The Golgi localization signal of RVF virus has been shown to reside within the GN protein by use of a plasmid-based transient expression system to synthesize individual GN and GC proteins. While the distribution of individually expressed GN significantly overlaps with cellular Golgi proteins such as β-COP and GS-28, GC expressed in the absence of GN localizes to the endoplasmic reticulum. Further analysis of expressed GN truncated proteins and green fluorescent protein/GN chimeric proteins demonstrated that the RVF virus Golgi localization signal mapped to a 48-amino-acid region of GN encompassing the 20-amino-acid transmembrane domain and the adjacent 28 amino acids of the cytosolic tail.

Documentos Relacionados

• Genetic Reassortment of Rift Valley Fever Virus in Nature
• Stability of Rift Valley fever virus at 4 C.
• Detection of Rift Valley fever virus antigen by enzyme-linked immunosorbent assay.
• Respiratory infectivity of a recently isolated Egyptian strain of Rift Valley fever virus.
• Use of bacterial expression cloning to define the amino acid sequences of antigenic determinants on the G2 glycoprotein of Rift Valley fever virus.