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Home / Equine Research Bank / Virology / Functional expression and membrane fusion tropism of the env...
Virology2002; 290(1); 121-135; doi: 10.1006/viro.2001.1158

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

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 alpha-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.
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Publication Date: 2002-03-09 PubMed ID: 11882997DOI: 10.1006/viro.2001.1158Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • U.S. Gov't
  • Non-P.H.S.

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The given research article discusses the studies conducted on the Hendra virus (HeV), an emerging paramyxovirus, focusing on the biological properties of the virus’s envelope glycoproteins. The investigation provides insights into the mechanisms of host cell infection and cross-species transmission, deepening our understanding of the risks posed by emerging pathogens.

Research Methodology

  • The researchers utilized recombinant vaccinia viruses that code for HeV’s F and G open reading frames to study the virus. The expression of glycoproteins was confirmed by metabolic labeling and detection using virus-specific antisera, which is a technique to label proteins and visualize them in a sensitive manner.
  • The functional role of the glycoproteins and the specific host cells they target were examined using a quantitative assay, specifically one designed to measure HeV-mediated membrane fusion. This process is critical for the virus’s ability to infect host cells.

Findings on Fusion Specificity

  • Through specific inhibitors like anti-HeV antiserum and a peptide corresponding to F’s alpha-helical heptad repeats, the scientists confirmed the specificity of the fusion process. This suggests that only the F and G glycoproteins are needed for the Hendra virus to fuse with host cells.

Identification of Permissive and Non-Permissive Cells

  • The researchers identified what cell lines the virus could infect. These cell types span many species, including cats, bats, horses, humans, monkeys, mice, and rabbits, revealing the broad host range of HeV.
  • The study also found cell types that did not fuse with the virus, indicating certain cells can resist HeV infection.

Implications for Target Receptor

  • The researchers found that protease treatments, which can degrade proteins on the surface of the cells, eliminated the ability of the virus to fuse with the cells. This suggests the Hendra virus relies on a specific protein on the cell surface to attach and enter the host cells.

Cite This Article

APA
Bossart KN, Wang LF, Eaton BT, Broder CC. (2002). Functional expression and membrane fusion tropism of the envelope glycoproteins of Hendra virus. Virology, 290(1), 121-135. https://doi.org/10.1006/viro.2001.1158

Publication

Virology
ISSN: 0042-6822
NlmUniqueID: 0110674
Country: United States
Language: English
Volume: 290
Issue: 1
Pages: 121-135

Researcher Affiliations

Bossart, K N
  • Department of Microbiology, Uniformed Services University, Bethesda, Maryland 20814, USA.
Wang, L F
    Eaton, B T
      Broder, C C

        MeSH Terms

        • 3T3 Cells
        • Amino Acid Sequence
        • Animals
        • Cell Line
        • Endopeptidase K
        • Giant Cells
        • HeLa Cells
        • Humans
        • Membrane Fusion / physiology
        • Membrane Glycoproteins / biosynthesis
        • Membrane Glycoproteins / metabolism
        • Membrane Glycoproteins / physiology
        • Mice
        • Molecular Sequence Data
        • Paramyxovirinae / metabolism
        • Paramyxovirinae / physiology
        • Trypsin
        • Viral Envelope Proteins / biosynthesis
        • Viral Envelope Proteins / physiology
        • Viral Fusion Proteins / biosynthesis
        • Viral Fusion Proteins / physiology

        Citations

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