期刊
JOURNAL OF VIROLOGY
卷 90, 期 1, 页码 245-253出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.02140-15
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资金
- HHS\ NIH \ National Institute of Allergy and Infectious Diseases (NIAID) [1R01AI087798, 1U19AI095227]
- Emory University
- CHOA [33515]
- NIH through Emory Vaccinology Training Grant [T32AI074492]
- Emory [33515]
- Emory through Nelson Memorial Fund [R6336510]
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.
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