Structural domains involved in human cytomegalovirus glycoprotein B-mediated cell-cell fusion
(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.
(Less)
- author
- Bold, S. ; Ohlin, M. LU ; Garten, W. and Radsak, K.
- organization
- publishing date
- 1996-09
- type
- Contribution to journal
- publication status
- published
- in
- Journal of General Virology
- volume
- 77
- issue
- 9
- pages
- 6 pages
- publisher
- Microbiology Society
- external identifiers
-
- pmid:8811030
- 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
- 2024-05-17 02:08:01
@article{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 = {{Microbiology Society}}, series = {{Journal of General Virology}}, title = {{Structural domains involved in human cytomegalovirus glycoprotein B-mediated cell-cell fusion}}, volume = {{77}}, year = {{1996}}, }