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Functional analysis of the Bunyamwera orthobunyavirus Gc glycoprotein.

Shi, Xiaohong; Goli, Josthna; Clark, Gordon; Brauburger, Kristina LU and Elliott, Richard M (2009) In Journal of General Virology 90(Pt 10). p.2483-2492
Abstract
The virion glycoproteins Gn and Gc of Bunyamwera orthobunyavirus (family Bunyaviridae) are encoded by the M RNA genome segment and have roles in both viral attachment and membrane fusion. To investigate further the structure and function of the Gc protein in viral replication, we generated 12 mutants that contain truncations from the N terminus. The effects of these deletions were analysed with regard to Golgi targeting, low pH-dependent membrane fusion, infectious virus-like particle (VLP) formation and virus infectivity. Our results show that the N-terminal half (453 residues) of the Gc ectodomain (909 residues in total) is dispensable for Golgi trafficking and cell fusion. However, deletions in this region resulted in a significant... (More)
The virion glycoproteins Gn and Gc of Bunyamwera orthobunyavirus (family Bunyaviridae) are encoded by the M RNA genome segment and have roles in both viral attachment and membrane fusion. To investigate further the structure and function of the Gc protein in viral replication, we generated 12 mutants that contain truncations from the N terminus. The effects of these deletions were analysed with regard to Golgi targeting, low pH-dependent membrane fusion, infectious virus-like particle (VLP) formation and virus infectivity. Our results show that the N-terminal half (453 residues) of the Gc ectodomain (909 residues in total) is dispensable for Golgi trafficking and cell fusion. However, deletions in this region resulted in a significant reduction in VLP formation. Four mutant viruses that contained N-terminal deletions in their Gc proteins were rescued, and found to be attenuated to different degrees in BHK-21 cells. Taken together, our data indicate that the N-terminal half of the Gc ectodomain is dispensable for replication in cell culture, whereas the C-terminal half is required to mediate cell fusion. A model for the domain structure of the Gc ectodomain is proposed. (Less)
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author
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of General Virology
volume
90
issue
Pt 10
pages
2483 - 2492
publisher
Society for General Microbiology
external identifiers
  • Scopus:70350489127
ISSN
1465-2099
DOI
10.1099/vir.0.013540-0
language
English
LU publication?
no
id
f6094803-cab3-41ce-a027-4309f814388c (old id 8726473)
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http://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=19570952&retmode=ref&cmd=prlinks
date added to LUP
2016-03-03 12:17:37
date last changed
2016-10-13 04:23:19
@misc{f6094803-cab3-41ce-a027-4309f814388c,
  abstract     = {The virion glycoproteins Gn and Gc of Bunyamwera orthobunyavirus (family Bunyaviridae) are encoded by the M RNA genome segment and have roles in both viral attachment and membrane fusion. To investigate further the structure and function of the Gc protein in viral replication, we generated 12 mutants that contain truncations from the N terminus. The effects of these deletions were analysed with regard to Golgi targeting, low pH-dependent membrane fusion, infectious virus-like particle (VLP) formation and virus infectivity. Our results show that the N-terminal half (453 residues) of the Gc ectodomain (909 residues in total) is dispensable for Golgi trafficking and cell fusion. However, deletions in this region resulted in a significant reduction in VLP formation. Four mutant viruses that contained N-terminal deletions in their Gc proteins were rescued, and found to be attenuated to different degrees in BHK-21 cells. Taken together, our data indicate that the N-terminal half of the Gc ectodomain is dispensable for replication in cell culture, whereas the C-terminal half is required to mediate cell fusion. A model for the domain structure of the Gc ectodomain is proposed.},
  author       = {Shi, Xiaohong and Goli, Josthna and Clark, Gordon and Brauburger, Kristina and Elliott, Richard M},
  issn         = {1465-2099},
  language     = {eng},
  number       = {Pt 10},
  pages        = {2483--2492},
  publisher    = {ARRAY(0x9ea3758)},
  series       = {Journal of General Virology},
  title        = {Functional analysis of the Bunyamwera orthobunyavirus Gc glycoprotein.},
  url          = {http://dx.doi.org/10.1099/vir.0.013540-0},
  volume       = {90},
  year         = {2009},
}