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Author Notes:

Address correspondence to Martin L. Moore, martin.moore@emory.edu.

We thank the Emory Children's Pediatric Research Center flow cytometry core supported by Children's Healthcare of Atlanta (CHOA).

We thank Edward Walsh for the monoclonal antibody to the RSV N protein and Ursula Buchholz and Karl-Klaus Conzelmann for the BSR-T7/5 cell line. We also thank Nancy Ulbrandt (MedImmune) for providing motavizumab antibody.

M.L.M. and Emory University are entitled to licensing fees derived from various agreements that Emory has entered into related to products used in this research described in this paper. This study could affect the personal financial status of M.L.M. The terms of this agreement have been reviewed and approved by Emory University in accordance with its conflict-of-interest policies.

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Research Funding:

HHS | NIH | National Institute of Allergy and Infectious Diseases (NIAID) provided funding to Michael M. Moore under grant numbers 1R01AI087798 and 1U19AI095227.

This study was also supported by funds from Emory University and CHOA.

Additional support was provided by the NIH through Emory Vaccinology Training Grant T32AI074492 (Christopher C. Stobart), by Emory and CHOA under joint grant number 33515 (Michael G. Currier, Christopher C. Stobart, Sujin Lee, and Martin L. Moore), and by Emory through Nelson Memorial Fund R6336510 (Anne L. Hotard and Martin L. Moore).

Keywords:

  • Science & Technology
  • Life Sciences & Biomedicine
  • Virology
  • HUMAN METAPNEUMOVIRUS FUSION
  • REPLICATION IN-VITRO
  • BALB/C MICE
  • IDENTIFICATION
  • ENTRY
  • INHIBITOR
  • HEPARIN
  • LACKING
  • SH
  • GLYCOSAMINOGLYCANS

Respiratory Syncytial Virus Attachment Glycoprotein Contribution to Infection Depends on the Specific Fusion Protein

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Journal Title:

Journal of Virology

Volume:

Volume 90, Number 1

Publisher:

, Pages 245-253

Type of Work:

Article | Final Publisher PDF

Abstract:

Human respiratory syncytial virus (RSV) is an important pathogen causing acute lower respiratory tract disease in children. The RSV attachment glycoprotein (G) is not required for infection, as G-null RSV replicates efficiently in several cell lines. Our laboratory previously reported that the viral fusion (F) protein is a determinant of strain-dependent pathogenesis. Here, we hypothesized that virus dependence on G is determined by the strain specificity of F. We generated recombinant viruses expressing G and F, or null for G, from the laboratory A2 strain (Katushka RSV-A2GA2F [kRSV-A2GA2F] and kRSV-GstopA2F) or the clinical isolate A2001/2-20 (kRSV-2-20G2-20F and kRSV-Gstop2-20F). We quantified the virus cell binding, entry kinetics, infectivity, and growth kinetics of these four recombinant viruses in vitro. RSV expressing the 2-20 G protein exhibited the greatest binding activity. Compared to the parental viruses expressing G and F, removal of 2-20 G had more deleterious effects on binding, entry, infectivity, and growth than removal of A2 G. Overall, RSV expressing 2-20 F had a high dependence on G for binding, entry, and infection.

Copyright information:

© 2015, American Society for Microbiology.

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