期刊
JOURNAL OF VIROLOGY
卷 81, 期 15, 页码 8361-8366出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.02717-06
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资金
- NIAID NIH HHS [R01 AI051372] Funding Source: Medline
Respiratory syncytial virus (RSV), a member of the Paramyxoviridae family, encodes a small hydrophobic (SH) protein of unknown function. Parainfluenza virus 5 (PIV5), a prototypical paramyxovirus, also encodes an SH protein, which inhibits tumor necrosis factor alpha (TNF-alpha) signaling. In this study, recombinant PIV5 viruses without their own SH but containing RSV SH (from RSV strain A2 or III) in its place (PIV5 Delta SH-RSV SH) and RSV lacking its own SH (RSV Delta SH) were generated and analyzed. The results indicate that the SH protein of RSV has a function similar to that of PIV5 SH and that it can inhibit TNF-alpha signaling.
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