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Identification of a linear heparin binding domain for human respiratory syncytial virus attachment glycoprotein G

S A Feldman1, R M Hendry, J A Beeler

  • 1Laboratory of Pediatric and Respiratory Virus Diseases, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, Maryland, USA. feldmans@cber.fda.gov

Journal of Virology
|July 10, 1999
PubMed

Insights

Respiratory syncytial virus (RSV) attachment protein G binds heparin via a specific domain, crucial for infection. This heparin-binding domain (HBD) on RSV G protein is key to viral entry and infectivity.

Area of Science:

  • Virology
  • Glycobiology
  • Molecular Biology

Background:

  • Respiratory syncytial virus (RSV) causes significant lower respiratory tract disease in young children globally.
  • RSV infection involves initial attachment protein (G) interaction with cell surface heparin-like glycosaminoglycans (Gag).

Purpose of the Study:

  • To identify and characterize the heparin-binding domain (HBD) of the RSV G protein.
  • To investigate the role of this HBD in viral attachment and infectivity.

Main Methods:

  • Synthetic peptides from RSV G protein ectodomain were tested for heparin binding using heparin-agarose affinity chromatography.
  • Peptide binding was assessed on Vero cells and CHO cell mutants deficient in Gag synthesis.
  • Inhibition of viral infectivity by HBD peptides was evaluated.

Main Results:

  • A single linear heparin-binding domain (HBD) was identified for RSV subgroup A (184A-->T198) and B (183K-->K197).
  • Peptide binding to cells was inhibited by heparin and significantly reduced in Gag-deficient cells.
  • RSV-G HBD peptides inhibited homologous and heterologous RSV infectivity.

Conclusions:

  • The identified sequence (184A/183K-->198T/K197) is a critical determinant of RSV-G interaction with heparin.
  • This HBD plays a significant role in RSV attachment and subsequent cell entry.

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