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Structural domains involved in human cytomegalovirus glycoprotein B-mediated cell-cell fusion

Bold, S.; Ohlin, M. LU ; Garten, W. and Radsak, K. (1996) In Journal of General Virology 77(9). p.2297-2302
Abstract

A novel fusion assay was established to determine fusion activity with cocultivated human foreskin fibroblasts of stable transfectants derived from human astrocytoma cells (U373) expressing authentic or mutagenized human cytomegalovirus glycoprotein B (HCMV gB; gpUL55). Compared to transfectants expressing authentic HCMV gB, those expressing gB forms with a deletion of hydrophobic domain 1 (hd1; aa 714-747) or with deletions of specific segments in the cytoplasmic tail (aa 811-825 and 871-906) exhibited significantly reduced heterologous fusogenicity. HCMV gB-specific monoclonal antibodies (MAbs) as well as MAb against cellular annexin II prevented fusion of the transfectant expressing authentic gB. Comparable surface exposure of HCMV... (More)

A novel fusion assay was established to determine fusion activity with cocultivated human foreskin fibroblasts of stable transfectants derived from human astrocytoma cells (U373) expressing authentic or mutagenized human cytomegalovirus glycoprotein B (HCMV gB; gpUL55). Compared to transfectants expressing authentic HCMV gB, those expressing gB forms with a deletion of hydrophobic domain 1 (hd1; aa 714-747) or with deletions of specific segments in the cytoplasmic tail (aa 811-825 and 871-906) exhibited significantly reduced heterologous fusogenicity. HCMV gB-specific monoclonal antibodies (MAbs) as well as MAb against cellular annexin II prevented fusion of the transfectant expressing authentic gB. Comparable surface exposure of HCMV gB or its derivatives was demonstrated in all transfectants by FAGS analysis. Our observations are compatible with the notion that indigenous fusion activity of HCMV gB depends on the extracellular hd1 domain and on the conformation of the cytoplasmic tail.

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author
organization
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type
Contribution to journal
publication status
published
in
Journal of General Virology
volume
77
issue
9
pages
6 pages
publisher
Society for General Microbiology
external identifiers
  • Scopus:0029817743
ISSN
0022-1317
language
English
LU publication?
yes
id
828d6809-4f6d-4b94-bbbc-43fa9c55b069
date added to LUP
2016-04-19 14:11:36
date last changed
2016-07-15 08:55:39
@misc{828d6809-4f6d-4b94-bbbc-43fa9c55b069,
  abstract     = {<p>A novel fusion assay was established to determine fusion activity with cocultivated human foreskin fibroblasts of stable transfectants derived from human astrocytoma cells (U373) expressing authentic or mutagenized human cytomegalovirus glycoprotein B (HCMV gB; gpUL55). Compared to transfectants expressing authentic HCMV gB, those expressing gB forms with a deletion of hydrophobic domain 1 (hd1; aa 714-747) or with deletions of specific segments in the cytoplasmic tail (aa 811-825 and 871-906) exhibited significantly reduced heterologous fusogenicity. HCMV gB-specific monoclonal antibodies (MAbs) as well as MAb against cellular annexin II prevented fusion of the transfectant expressing authentic gB. Comparable surface exposure of HCMV gB or its derivatives was demonstrated in all transfectants by FAGS analysis. Our observations are compatible with the notion that indigenous fusion activity of HCMV gB depends on the extracellular hd1 domain and on the conformation of the cytoplasmic tail.</p>},
  author       = {Bold, S. and Ohlin, M. and Garten, W. and Radsak, K.},
  issn         = {0022-1317},
  language     = {eng},
  number       = {9},
  pages        = {2297--2302},
  publisher    = {ARRAY(0x90c7030)},
  series       = {Journal of General Virology},
  title        = {Structural domains involved in human cytomegalovirus glycoprotein B-mediated cell-cell fusion},
  volume       = {77},
  year         = {1996},
}