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Document A. IFN-τ Synthetic Peptide Studies Page 440 A sheep blastocyst library was screened with a probe based on the N-terminal sequence of the IFN-τ protein and the cDNA obtained (Table 3). Surprisingly, it exhibited 45–55% homology with various IFNs from human, mouse, rat, and pig and 70% homology with bovine IFN-ω [12]. It shared both molecular weight (19 kDa) and pI (5.4–5.6) with IFN-αs, while its length, 172 amino acids, was equivalent to the IFN-ωs. In competition studies, IFN-τ was found to compete with IFNs α, β, and ω for binding to the Type I IFN receptor [13]. In contrast, IFN-τ exhibited several unique properties such as its reproductive function, its poor inducibility by virus, and its apparent reduced cytotoxicity. Thus, IFNτ conceptus protein appears to be a novel IFN. Structural studies began with production of overlapping synthetic peptides, each 30–35 amino acids in length, corresponding to the entire http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_440.html (1 of 2) [4/9/2004 12:11:03 AM]
Document Page 441 sequence of the molecule [14]. The peptides were used in competition assays with the native molecule. Peptide inhibition of a particular function would implicate the region of the molecule that it represented in the elicitation of that function. The effect of the IFN-τ peptides on the antiviral activity of ovine IFNτ was examined in a dose/response assay using Madin Darby bovine kidney (MDBK) cells challenged with vesicular stomatitis virus. The carboxy-terminal peptide oIFN-τ(139–172) was found to be the most effective inhibitor of antiviral activity. Three additional peptides, oIFN-τ(1–37), (62–92), and (119–150), also reduced IFN-τ antiviral activity. This suggested that multiple regions of the IFN-τ molecule interact with the Type I IFN receptor and elicit antiviral activity. These regions are underlined in Table 3. The data were consistent with studies of antiviral activity and receptor binding with IFN-α analogs demonstrating that 3 distinct sites, located in the amino-terminal, internal, and carboxy-terminal regions of the molecule, influenced human IFN-α activity [15]. To verify functional results using synthetic peptides, antipeptide antisera were produced [14]. All antipeptide antisera were reactive with the native molecule. Interestingly, antisera titers correlated with the hydropathic index of the peptide, rather than with the predicted surface accessibility of the specific region in the 3-D configuration. Consistent with the peptide studies, antisera against the same four regions of the molecule inhibited IFN-τ activity while antisera to other regions did not. Since IFN-τ and IFN-α bind to the same receptor, the ability of the IFN-τ synthetic peptides to block both bovine and human IFN-α was examined. Interestingly, only three of the four inhibitory peptides were effective competitors of IFN-α. Cross-inhibition of IFN-α by the internal and carboxy-terminal peptides was observed and suggested that these residues may adopt a similar conformation in both molecules and bind to a common site on the receptor. The aminoterminal peptide failed to reduce IFN-α function entirely. Thus, either the IFN-α amino-terminus has a much higher affinity for receptor or the IFN-τ aminoterminus binds a unique site on the receptor complex that may be associated with its unique properties. As expected, none of the peptides blocked the antiviral activity of IFN-τ, which interacts with a different receptor. Next, it was determined whether the same active regions of IFN-τ were involved in additional systems. The Type I IFN receptor on cells has been reported to be somewhat more promiscuous than on other cell types [16]; therefore, vesicular stomatitis challenge of Fc-9 cells was performed. Only the carboxyterminal peptide inhibited IFN-τ activity in this system [17]. This suggested that it was the carboxyterminus that was crucial to receptor interaction. In studies examining IFN-τ-treated feline immunodeficiency virus infected FeT-1 cells and human immunodeficiency virus-infected peripheral http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_441.html [4/9/2004 12:11:10 AM]
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Document Page 72 16. Goldman ME, Nu
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Document Page 108 mulate during tre
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Document 6 Structural Implications
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Page 537 and 538: Document 74. Bender PE, Lee JC., ed
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Page 541 and 542: Document 17 Structure and Functiona
Page 543 and 544: Document Table 1 Approval Indicatio
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Page 553 and 554: Document Figure 4 Stereo view of IF
Page 555 and 556: Document Figure 5 Velcro-key model
Page 557 and 558: Document Figure 6 Proposed receptor
Page 559 and 560: Document Page 451 with the cytoplas
Page 561 and 562: Document for directed subcellular t
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Page 579 and 580: Document B. Protein Structure Page
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Page 583 and 584: Document Page 471 molecules in the
Page 585 and 586: Document hydroxy, and 6 Neu5Ac2en -
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Page 589 and 590: Document Page 476 nM, respectively.
Page 591 and 592: Document Page 478 lished—was asso
Page 593 and 594: Document VI. Conclusion Page 480 It
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Document D ddI, 152 tumour necrosis
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Document antistasin peptides, 281 c
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