Role of the Cytoplasmic Tail Domains of Bunyamwera Orthobunyavirus Glycoproteins Gn and Gc in Virus Assembly and Morphogenesis.

Xiaohong Shi, A Kohl, P Li, Richard Michael Elliott

Research output: Contribution to journalArticlepeer-review

59 Citations (Scopus)

Abstract

The M RNA genome segment of Bunyamwera virus (BUNV), the prototype of the Bunyaviridae family, encodes a precursor polyprotein that is proteolytically cleaved to yield two structural proteins, Gn and Ge, and a nonstructural protein called NSm. Gn and Gc are type I integral transmembrane glycoproteins. The Gn protein contains a predicted cytoplasmic tail (CT) of 78 residues, and Gc has a shorter CT of 25 residues. Little is known about the role of the Gn and Gc CT domains in the virus replication cycle. We generated a series of mutant glycoprotein precursor constructs containing either deletions or alanine substitutions in the CT domains of Gn and Gc. We examined the effects of these mutations on glycoprotein maturation, cell surface expression, and low pH-induced syncytium formation. In addition, the effects of these mutations were also assessed using a reverse genetics-based virus assembly assay and a virus rescue system. Our results show that the CT domains of both Gn and Gc play crucial roles in BUNV-mediated membrane fusion, virus assembly, and morphogenesis.

Original languageEnglish
Pages (from-to)10151-10160
Number of pages10
JournalJournal of Virology
Volume81
Issue number18
DOIs
Publication statusPublished - Sept 2007

Keywords

  • CELL-FUSION
  • UUKUNIEMI-VIRUS
  • MINIREPLICON SYSTEM
  • MEMBRANE-FUSION
  • INFLUENZA-VIRUS
  • GOLGI-COMPLEX
  • PROTEIN
  • HANTAVIRUS
  • BUNYAVIRUS
  • MATURATION

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