A polyphenolic complex (PC), isolated from the Bulgarian medicinal plant Germanium sanguineum L., inhibited the reproduction of influenza virus types A and B in vitro and in ovo. HSVs deleted of gE, gG, gI, gJ, gM, UL45, or Us9 entered cells via either pH-dependent or pH-independent endocytosis and were inactivated by mildly acidic pH. These viruses are known to infect the host cells by causing the fusion of viral and host cell membrane proteins. J. vhs residues 238 to 344 were sufficient for the interaction, and the VP16 acidic transcriptional activation domain was not required. Of seven mutants analyzed by an in vivo replication assay, three mutants, in three different conserved regions of the protein, failed to support DNA replication. Instead, inserted DNA was found to hybridize to HindIII-digested cellular DNA as a single or double band in 5 plasmids and contained multiple repeat sequences such as alpha satellite, Alu or Kpn repeats in 4 plasmids.
Recent experiments showed that Vhs interacts with the cellular translation initiation factor eIF4H. In this study, the coexpression of Vhs and a glutathione S-transferase (GST)-eIF4H fusion protein in bacteria resulted in the formation of a complex of the proteins. Extensive mutagenesis of the HSV-1 gB ectodomain reveals remarkable stability of its postfusion form. The EBV complex comprised of BFRF1 and BFLF2 was visualized at the nuclear membrane using autofluorescent protein fusions. Mol. The chemical nature of the RNA primer was proven by degradation experiments with endoribonuclease V. Furthermore, only oligonucleotides containing primase templates were inhibitory in a coupled primase-polymerase assay using X174 DNA as template, suggesting that primer synthesis or primase turnover is rate-limiting.
PMC3655159. Silverman J.L., Greene N.G., King D.S., and Heldwein E.E. (2012). Class III fusion proteins contain a central triple coiled coil reminiscent of the class I fusion proteins. J. BAY 57–1293, now known as pritelivir (AIC316, Aicuris®) has also revealed a potent in vitro/in vivo anti-herpetic activity when compared to VACV ( Baumeister et al., 2007, Biswas et al., 2007a and Kleymann et al., 2002). 86, 8171-8184.
HuIL-6 exhibits a wide spectrum of biological activities, including mediation of fever and acute phase inflammatory response to trauma and pathogens, stimulation of osteoclast formation, and promotion of neuronal regeneration (5). Eisenberg R.J., Heldwein E.E., Cohen G.H., and Krummenacher C. Recent progress in understanding herpes simplex virus entry: relationship of structure to function. In: “Alpha Herpesviruses: Molecular Virology”, S.K. Therefore, interactions between the cytoplasmic domains of gE/gI and the AP-1 cellular sorting machinery cause glycoprotein accumulation and envelopment into specific TGN compartments that are sorted to lateral cell surfaces. Caister Academic Press. The multitude of tegument proteins have different locations within the cell; some are exclusively cytoplasmic and others exclusively nuclear, and yet others are detected in both compartments.
Cairns T.M., Whitbeck J.C., Lou H., Heldwein E.E., Chowdary T.K., Eisenberg R.J., and Cohen G.H. (2011). Titers on Vero cells were set to 100%. J. Virol. 85, 6175-6184. PMC3126480.
Stampfer S.D., Lou H., Cohen G.H., Eisenberg R.J., and Heldwein E.E. (2010). In particular, nine charged or hydrophilic residues are highly conserved between Vhs and the cellular nucleases. J. For both the PRV and HSV-1 NEC, the interaction domains that are important for mediating complex formation have been mapped and the roles of the transmembrane (TM) region in UL34 and the UL34 C terminus have been determined (28, 32, 33, 60). 84, 12924-12933. PMC3004323.
Radiolabeled primers were extended during incubation at 37°C for 60 min. (2010). Crystal structure of the conserved herpesvirus fusion regulator complex gH–gL. Nat. This interaction may mimic that formed upon endosome acidification during entry. Mol. Biol.
17, 882-888. The second, but not mutually exclusive, hypothesis was that N-linked sugars on Asn-89 were required for proper protein folding. Bender F.C., Samanta M., Heldwein E.E., deLeon M.P., Lou H., Bilman E., Whitbeck J.C., Eisenberg R.J., and Cohen G.H. (2007). Antigenic and mutational analyses of herpes simplex virus glycoprotein B reveal four functional regions. J. Virol.
The PCR product was digested with SpeI (underlined sequence) and cloned in the correct orientation into the pKBD plasmid, also cut with SpeI. Vazquez-Laslop N., Zheleznova E.E., Markham P.N., Brennan R.G., and Neyfakh A.A. (2000). Error bars indicate standard deviations. Biochem. Soc. Trans.
28, 517-520. Zheleznova E.E., Markham P.N., Neyfakh A.A., and Brennan R.G. (1997). Cultures were transfected with 0.6-ml aliquots containing calcium phosphate coprecipitates of 3 μg of the reporter plasmid pSV-β-galactosidase (Promega) and 0.73 pmol of either a UL41-containing effector plasmid or the expression vector pcDNA1.1amp. Protein Science 6, 2465-2468. ORF67 and ORF69 sequences were also transferred from the plasmids carrying C-terminal V5, HA, GFP, and mCherry tags into pcDNA 3.1(−) (Invitrogen) using EcoRI and HindIII digestion. (1997).
Allosteric Intermediates Indicate R2 is the Liganded Hemoglobin End State. A, nondenaturing 4% PAGE of restriction fragments of X174 DNA initiated with radiolabeled primers. Natl. Acad. Sci. To neutralize proteins from pH 5 to pH 7, we added 1 M Tris (pH 8.0) postincubation.