On infection, the herpes simplex virus (HSV) virion protein VP16 (Vmw65; alphaTIF) forms a transcriptional regulatory complex-the VP16-induced complex-with two cellular proteins, HCF and Oct-1, on VP16-responsive cis-regulatory elements in HSV immediate-early promoters called TAATGARAT. The compounds were prepared by the condensation of 2-acetylpyridine with thiocarbonohydrazide followed by treatment with isocyanates or isothiocyanates. Although K(b) and K(bm8) differ by four residues within the Ag-binding cleft, the most striking difference in the two structures was the disparate conformation adopted by the shared residue, Arg(62). When VH and VL regions of mAb II-481 were synthesized as overlapping 7-mer peptides on polypropylene pins, a panel of 10 polyclonal and 6 monoclonal human IgM RFs reacted primarily with epitopes within the three solvent-exposed mAb II-481 complementarity determining regions (CDRs). Natl. We determined the abilities of the gD mutants to bind receptors, facilitate virus entry, and mediate cell-cell fusion. The virus-induced destabilizing activity had no significant effect on the in vitro half-lives of two normally unstable mRNAs, histone and c-myc.
USA 86:6518-6522, 1989). The protein reacts with both DNA and RNA in band-shift assays and protects the single-stranded RNA sequence from digestion by RNase. We report that the minimal cognate sequence required for these interactions consisted of [N(GTGGGTGGG)2(N less than or equal to 10)]. The ninemer repeat sequence was located at nucleotides -1 to -18 relative to the transcription initiation of the major species of OriSRNA. ► Zinc oxide tetrapods as virus trapping agents. Taken together, these results constitute the first demonstration of VS-dependent cell-to-cell spread for a predominantly nonlymphotropic virus. Here, we report the crystal structures of HSV-2 gD in both the free and the nectin-1-bound forms.
The monoclonal antibody to this protein, CH28-2, was purchased from the Goodwin Cancer Research Institute (Plantation, Fla.). Many aspects of capsid assembly and DNA packaging in the herpesviruses are similar to those in dsDNA bacteriophages such as λ, T4, and P22 (7, 42). The potential role of a functional LAT-encoded protein during HSV latency, first suggested by Wilcox and coworkers (11), has largely been discounted, not least due to the lack of a consistent phenotype when the LAT ORFs are mutated (19, 21) and the fact that no LAT-encoded proteins have been reliably detected in latently infected neurons (11, 38). The HveA … Links to PubMed are also available for Selected References.