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FIGURE 15.5 Titers of VV WR in tissues after intranasal inoculation: 4-week-old C57BL/6 mice were infected with 106 pfu of VV WR. Tissues were harvested 5 days postinfection and titered on RK-13 cells.
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observed with the P63A mutation. Corresponding residues in ADAR1 result in a reduced af nity for Z-DNA. Of the two prolines, the ADAR1 equivalent residue to E3L P63 is more essential for high-af nity Z-DNA binding, therefore reinforcing the correlation of Z-DNA binding with pathogenicity of vaccinia virus. As shown with the Z-DNA binding mutants, what is known about the N terminus of E3L is the requirement of this domain, as well as the C-terminal dsRNA binding domain, in viral pathogenesis. In C57Bl6 mice, wild-type vaccinia virus replicates to high titers in nasal tissue upon intranasal inoculation and then spreads to the lungs and brain (Figure 15.5). Animals apparently die of encephalitis 5 8 days postinfection. Vaccinia virus deleted of E3L or of the dsRNA binding domain replicate poorly in the nasal tissue, no virus is detected in the lungs or brain, and infected animals show no signs of illness. Virus that still encodes the dsRNA domain but is deleted for the N terminus of E3L replicates to wild-type levels in the nasal mucosa but fails to spread. This virus is more pathogenic than a full E3L deletion but is at least 1000-times less pathogenic than wild-type virus. As mentioned before, the dsRNA binding activity associated with E3L is much more well understood. More than 20 functionally distinct proteins containing the conserved dsRNA binding motif have been identi ed.82 Over the years, mutational analysis of E3L and other proteins containing this conserved motif of 65 68 amino acids has revealed many of the residues required for high-af nity binding to
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THE E3L GENE
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PKR-1 VV WR E3L ADAR-1 RNASE III STAUFEN-2 TN RNA BP Consensus
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-FFMEELNTYRQKQGVVLKYQELPNSGPPHDRRFTFQVIIDGREFPEGEGRSKKEAKNAAAKLAVEILN -NPVTVINEYCQITRRDWSFR-IESVGPSNSPTFYACVDIDGRVFDKADGKSKRDAKNNAAKLAVDKLL -NPISGLLEYAQFASQTCEFNMIEQSGPPHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAMKAMTILL -QLQEIVQRDRDVL---IEYDILGETGPAHNKAFDAQVIVNGQVLGKGSGRTKKQAEQSAAQFAINKLI -SEISQVFEIALKRNLPVNFEVARESGPPHMKNFVTKVSV-GEFVGEGEGKSKKISKKNAAIAVLEELK -NPVSALHQFAQMQRVQLDLKETVTTGNVMGPYFAFCAVVDGIQYKTGLGQNKKESRSNAAKLALDELL NP NEYCQ T R F G H P F V I G F A G SKK A AA A LL
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FIGURE 15.6 dsRNA binding domain homology of E3L to select cellular dsRNA binding proteins. PKR: human dsRNA-dependent protein kinase (domain 1); VV WR-E3L: vaccinia virus E3L; ADAR1: human RNA-speci c adenosine deaminase (domain 1); RNase III: Listeria monocytogenes; Staufen-2: human Staufen-2 (domain 2); TN RNA BP: testis nuclear dsRNA binding protein from Mus musculus.
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dsRNA. The E3L protein binds dsRNA molecules in a sequence-independent manner with a Kd ~ 7 9 nm.82 The dsRNA binding domain of E3L shares signi cant homology to dsRNA domains identi ed on many cellular proteins (Figure 15.6). This domain on E3L shares the greatest homology with the ADAR protein, followed by the testis nuclear RNA binding protein and PKR. Substitutions at six conserved residues present on the same face of the binding motif, Glu-124, Phe-135, Phe-148, Lys-167, Arg-168, and Lys-171, greatly reduce dsRNA af nity, and are therefore likely part of the RNA binding site.82 Although the structure of E3L has not yet been elucidated, relevance regarding the structure of the E3L dsRNA binding motif can be inferred based on structural data from similar domains present on other proteins. F or PKR, which contains two tandem motifs, the structure reveals a dumb-bell shape with each motif having an a b b b a fold.83 Similar motif folds were demonstrated for Staufen and RNase III.84 86 The dsRNA recognition mechanism involves interactions with the 20 -OH groups present in the minor groove of the RNA duplex and the dsRNA binding domain.87 When bound to the 20 -OH groups through hydrogen bonding, positively charged residues (equivalent to Lys-167 in E3L) likely make electrostatic interactions with the negatively charged phosphate backbone on the RNA duplex. For PKR, the linker region between the dsRNA binding motifs is highly exible, which allows the two motifs to wrap around the RNA duplex for cooperative and high-af nity binding.83 For E3L, two RNA binding motifs are presented after protein dimerization. In recent years, the structure of the dsRNA binding motif complexed with dsRNA has been resolved. The structure reveals that an RNA duplex of 12 16 base pairs is necessary for binding.88,89 Interaction involves recognition of two successive minor grooves and spanning across the intervening major groove on one face of the RNA duplex. This manner of interaction explains the nonsequence-speci c recognition of dsRNA and lack of binding to ssRNA or dsDNA. Of the a b b b a motif, the N terminus of a1 and the loop between b1 and b2 interact with the adjacent minor grooves on the RNA duplex and a2 interacts with the intervening major groove.89,90 Considering corresponding conserved residues in E3L, it is likely that Glu-122 in a1, and Lys-167 and Lys-171 in a2 are involved in direct interaction with the RNA duplex.
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