Functional expression and membrane fusion tropism of the envelope glycoproteins of Hendra virus

Katharine N. Bossart, Lin Fa Wang, Bryan T. Eaton, Christopher C. Broder*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

87 Scopus citations

Abstract

Hendra virus (HeV) is an emerging paramyxovirus first isolated from cases of severe respiratory disease that fatally affected both horses and humans. Understanding the mechanisms of host cell infection and cross-species transmission is an important step in addressing the risk posed by such emerging pathogens. We have initiated studies to characterize the biological properties of the HeV envelope glycoproteins. Recombinant vaccinia viruses encoding the HeV F and G open reading frames were generated and glycoprotein expression was verified by metabolic labeling and detection using specific antisera. Glycoprotein function and cellular tropism were examined with a quantitative assay for HeV-mediated membrane fusion. Fusion specificity was verified through specific inhibition by anti-HeV antiserum and a peptide corresponding to one of the α-helical heptad repeats of F. HeV requires both F and G to mediate fusion. Permissive target cells have been identified, including cell lines derived from cat, bat, horse, human, monkey, mouse, and rabbit. Fusion negative cell types have also been identified. Protease treatments of the target cells abolished fusion activity, suggesting that the virus is employing a cell-surface protein as its receptor.

Original languageEnglish
Pages (from-to)121-135
Number of pages15
JournalVirology
Volume290
Issue number1
DOIs
StatePublished - 10 Nov 2001

Keywords

  • Envelope glycoprotein
  • Fusion
  • Hendra virus
  • Nipah virus
  • Paramyxovirus
  • Receptor
  • Tropism

Cite this