Author: Joshua A. Hayward; Mary Tachedjian; Adam Johnson; Tamsin B. Gordon; Jie Cui; Glenn A. Marsh; Michelle L. Baker; Lin-Fa Wang; Gilda Tachedjian
Title: Bats Possess Unique Variants of the Antiviral Restriction Factor Tetherin Document date: 2020_4_9
ID: eksi9yia_11
Snippet: The dual-tyrosine Y·x·Y motif, which is critical for mediating viral-particle endocytosis and is involved in immune signaling cascades (25, 34), is variable among bat species and exists in various combinations of Y|C·x·Y|H ( Figure 1A and 1C). All bat species possess at least one tyrosine residue within this motif ( Figure 1C) . Conservation of the protein domain organization and key structural motifs of bat tetherin, despite significant amin.....
Document: The dual-tyrosine Y·x·Y motif, which is critical for mediating viral-particle endocytosis and is involved in immune signaling cascades (25, 34), is variable among bat species and exists in various combinations of Y|C·x·Y|H ( Figure 1A and 1C). All bat species possess at least one tyrosine residue within this motif ( Figure 1C) . Conservation of the protein domain organization and key structural motifs of bat tetherin, despite significant amino acid sequence diversity, supports the present understanding of tetherin as a protein whose functions are mediated through structural rather than sequence-mediated interactions (22) .
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