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Human herpesvirus-8 glycoprotein B interacts with Epstein-Barr virus (EBV) glycoprotein 110 but fails to complement the infectivity of EBV mutants.

Abstract
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 gamma-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.
AuthorsP E Pertel, P G Spear, R Longnecker
JournalVirology (Virology) Vol. 251 Issue 2 Pg. 402-13 (Nov 25 1998) ISSN: 0042-6822 [Print] United States
PMID9837804 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)
CopyrightCopyright 1998 Academic Press.
Chemical References
  • DNA, Viral
  • Epstein-Barr virus glycoprotein gp110
  • Viral Envelope Proteins
  • Viral Proteins
  • glycoprotein B, Simplexvirus
  • glycoprotein B, human herpesvirus 7
Topics
  • Amino Acid Sequence
  • Animals
  • Blotting, Western
  • CHO Cells
  • Cricetinae
  • DNA, Viral (genetics)
  • Glycosylation
  • Herpesvirus 4, Human (genetics, pathogenicity)
  • Herpesvirus 8, Human (genetics, metabolism)
  • Humans
  • Molecular Sequence Data
  • Open Reading Frames
  • Viral Envelope Proteins (chemistry, genetics, metabolism)
  • Viral Proteins

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