TY - JOUR
T1 - Human herpesvirus-8 glycoprotein B interacts with Epstein-Barr virus (EBV) glycoprotein 110 but fails to complement the infectivity of EBV mutants
AU - Pertel, Peter E.
AU - Spear, Patricia G.
AU - Longnecker, Richard
N1 - Funding Information:
We thank Lola Kwan for assistance with PCR and John Phair for supplying specimens from the Multicenter AIDS Cohort Study. P.E.P. was supported by a grant from the National Institutes of Health (K08 AI-01405). This work was supported in part by research grants CA62234 (R.L.), CA73507 (R.L.), and CA21776 (P.G.S.) from the National Cancer Institute, U.S. Public Health Service. R.L. is a Scholar of the Leukemia Society of America.
PY - 1998/11/25
Y1 - 1998/11/25
N2 - To characterize human herpesvirus 8 (HHV-8) gB, the open reading frame was PCR amplified from the HHV-8-infected cell line BCBL-1 and cloned into an expression vector. To facilitate detection of expressed HHV-8 gB, the cytoplasmic tail of the glycoprotein was tagged with the influenza hemagglutinin (HA) epitope. Expression of tagged HHV-8 gB (gB-HA), as well as the untagged form, was readily detected in CHO-K1 cells and several lymphoblastoid cell lines (LCLs). HHV-8 gB-HA was sensitive to endoglycosidase H treatment, and immunofluorescence revealed that HHV-8 gB- HA was detectable in the perinuclear region of CHO-K1 cells. These observations suggest that HHV-8 gB is not processed in the Golgi and localizes to the endoplasmic reticulum or nuclear membrane. Because both HHV- 8 and EBV are γ-herpesviruses, the ability of HHV-8 gB to interact with and functionally complement EBV gp110 was examined. HHV-8 gB-HA and EBV gp110 co- immunoprecipitated, indicating formation of hetero-oligomers. However, HHV-8 gB-HA and HHV-8 gB failed to restore the infectivity of gp110-negative EBV mutants. These findings indicate that although HHV-8 gB and EBV gp110 have similar patterns of intracellular localization and can interact, there is not sufficient functional homology to allow efficient complementation.
AB - To characterize human herpesvirus 8 (HHV-8) gB, the open reading frame was PCR amplified from the HHV-8-infected cell line BCBL-1 and cloned into an expression vector. To facilitate detection of expressed HHV-8 gB, the cytoplasmic tail of the glycoprotein was tagged with the influenza hemagglutinin (HA) epitope. Expression of tagged HHV-8 gB (gB-HA), as well as the untagged form, was readily detected in CHO-K1 cells and several lymphoblastoid cell lines (LCLs). HHV-8 gB-HA was sensitive to endoglycosidase H treatment, and immunofluorescence revealed that HHV-8 gB- HA was detectable in the perinuclear region of CHO-K1 cells. These observations suggest that HHV-8 gB is not processed in the Golgi and localizes to the endoplasmic reticulum or nuclear membrane. Because both HHV- 8 and EBV are γ-herpesviruses, the ability of HHV-8 gB to interact with and functionally complement EBV gp110 was examined. HHV-8 gB-HA and EBV gp110 co- immunoprecipitated, indicating formation of hetero-oligomers. However, HHV-8 gB-HA and HHV-8 gB failed to restore the infectivity of gp110-negative EBV mutants. These findings indicate that although HHV-8 gB and EBV gp110 have similar patterns of intracellular localization and can interact, there is not sufficient functional homology to allow efficient complementation.
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U2 - 10.1006/viro.1998.9412
DO - 10.1006/viro.1998.9412
M3 - Article
C2 - 9837804
AN - SCOPUS:0032567118
SN - 0042-6822
VL - 251
SP - 402
EP - 413
JO - Virology
JF - Virology
IS - 2
ER -