By analogy to well-characterized bacteriophage systems, the association of these proteins with various forms of capsids, including procapsids, might be expected to clarify their roles in the packaging process. PDTC suppressed the expression of HSV-1 and HSV-2 viral immediate early (IE) and late (membrane protein gD) genes and the production of viral progeny. p32 formed a complex(es) with HSV-1 proteins UL31, UL34, Us3, UL47, and/or ICP22 in HSV-1-infected cells. IgG antibodies to CMV and C pneumoniae were also measured in the serum. With this assay, we have observed a high frequency of recombination (approximately 8%) in plasmids that undergo replication in HSV-1-infected cells. In C57BL/6 mice, the immunodominant epitope from HSV is derived from glycoprotein B (gB498-505). The present report reevaluates the molecular mimicry hypothesis to explain HSK pathogenesis.
Mapping of the gF gene was done by insertion of HSV-2 DNA fragments into the thymidine kinase gene of an HSV-1 virus and screening of the resultant recombinant viruses for the expression of gF. On this basis, it was proposed that a main route of capsid exit from the nucleus is directly through these altered pores. We confirmed the inhibitory effects of NFV on HSV-1 replication by plaque assay and found that treatment with NFV did not affect capsid assembly, activity of the HSV-1 maturational protease, or formation of DNA-containing capsids in the nucleus. Because gB has a role in attachment and entry of HSV, we tested the effects of ISIS 5652 at these stages of infection. In an attempt to further localize the point in the HSV-1 replication cycle where arrest occurred, a set of key regulatory events leading to viral multiplication was examined, including viral immediate-early (α), early (β), and late (γ) gene expression and DNA replication. Little or no increase in the maturation marker CD83 was observed in response to HSV-2 and HSV-2 exposed DCs were impaired in their ability to present antigen (influenza) to T cells. The “moving wall” represents the time period between the last issue available in JSTOR and the most recently published issue of a journal.
To test this, we created a recombinant HSV-1 in which gB is expressed only after viral DNA synthesis from the true late gC promoter (gCp-gB). PKCα was less dramatically relocalized mostly at the nuclear rim upon infection, although some PKCα remained in the cytoplasm. S. Although several of the polymers have advanced to clinical trials, the spectrum and mechanism of anti-HSV activity and the effects on soluble mediators of inflammation have not been evaluated. In the multicomponent herpesvirus fusion machinery, glycoprotein B (gB) acts as this fusogen. This is largely due to the misfolding of the majority of the mutants examined. They failed, however, to form plaques and to synthesize virus-specific proteins upon infection.
In C57BL/6 mice, the immunodominant epitope from HSV is derived from glycoprotein B (gB(498-505)). In current models, gC and/or gB binds cell surface heparan sulfate proteoglycans, bringing the viral envelope and plasma membrane close enough for fusion to occur (69). Although several of the polymers have advanced to clinical trials, the spectrum and mechanism of anti-HSV activity and the effects on soluble mediators of inflammation have not been evaluated. Members of both classes accomplish fusion through a large-scale conformational change, triggered by a signal from a receptor-binding component. However, cells deficient in proteoglycan synthesis can still be infected by HSV. To test the hypothesis that glycoprotein B (gB), the other heparin-binding glycoprotein, mediates HSV-2 attachment, HSV-2 viruses deleted in gB-2 alone or deleted in both gB-2 and gC-2 were constructed. At 20 hr after challenge, immunostaining of virus proteins in the vaginal epithelium and shed virus protein titres in the vaginal secretions were not significantly different between immunized and non-immunized B-cell KO mice and were much greater than in immunized intact mice.
The cytoplasmic domain of gB, the longest one among HSV-1 glycoproteins, contains several highly conserved peptide sequences homologous to motifs involved in intracellular sorting. With regard to infectious agents, speculation has often centered on the neurotropic herpes viruses, with herpes simplex virus 1 (HSV1) considered a likely candidate. The fusion protein was used to generate anti-US11 monoclonal antibody. Absence of either IKK1 or IKK2 resulted in an 86 to 94% loss of virus yield compared to that of normal MEFs, little or no loss of IκBα, and greatly reduced NFκB nuclear translocation. A similar multiplicity dependence for growth and lack of virus spread at low multiplicity was seen in resting, confluent human embryonic lung (HEL) cells. In the first, temperature-sensitive mutants of HSV-1 and HSV-2 were crossed to produce wild-type recombinants. The precursor pgF was sensitive to endoglycosidase H digestion, indicating the presence of high mannose-type oligosaccharides, whereas the stable gF product was sensitive to neuraminidase digestion, indicating the presence of sialic acid residues.
Glycoprotein B (gB) of herpes simplex virus type 1 (HSV-1) binds to PILRalpha, and this association is involved in HSV-1 infection.