Author: Shields, Lauren E.; Jennings, Jordan; Liu, Qinfang; Lee, Jinhwa; Ma, Wenjun; Blecha, Frank; Miller, Laura C.; Sang, Yongming
Title: Cross-Species Genome-Wide Analysis Reveals Molecular and Functional Diversity of the Unconventional Interferon-? Subtype Document date: 2019_6_25
ID: 14gcu1se_40
Snippet: buffer at pH 2.0 for 24 h at 4 • C. Incubation of IFN peptides in acidic buffer caused almost no loss in antiviral activity against PRRSV infection in MARC-145 cells ( Table 1 ). In contrast, high temperatures at 42, 56, or 63 • C for 5 h removed all activity of the IFN-α peptide; however, IFN-ω peptides showed better thermal stability. IFN-ω1 retained most active after treated at 42 • C, IFN-ω5 retained much activity even when treated .....
Document: buffer at pH 2.0 for 24 h at 4 • C. Incubation of IFN peptides in acidic buffer caused almost no loss in antiviral activity against PRRSV infection in MARC-145 cells ( Table 1 ). In contrast, high temperatures at 42, 56, or 63 • C for 5 h removed all activity of the IFN-α peptide; however, IFN-ω peptides showed better thermal stability. IFN-ω1 retained most active after treated at 42 • C, IFN-ω5 retained much activity even when treated at 56 or 63 • C for 5 h ( Table 1) . We also examined the acidic and thermal stability using a more sensitive ISG-promoter reporter luciferase assay and observed similar results as that of the antiviral assay (data not shown) (13, 23) . Hence, porcine IFN-ω peptides exert better thermal stability but similar acidic stability compared to IFN-α peptide (20, 25) .
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