Phosphorylation of Bovine Herpesvirus 1 VP8 Plays a Role in Viral DNA Encapsidation and Is

Additional studies are required for a better understanding of the mechanism of action of PLS and β-glucan. Our results indicated that the replication of BHV-1 in semi-permissive HmLu-1 was not dramatically restricted at one certain point but at some various stages including adsorption and penetration. These hormone-related findings are important since herpesvirus infections at the genital site are known to be influenced by reproductive hormone levels [25]. The results indicate that phosphorylated VP8 plays a role in viral DNA encapsidation and in the secondary virion incorporation of VP8. 71:8886-8892, 1997). Calves latently infected with the 51g mutant did not reactivate from latency because virus shedding did not occur in ocular or nasal cavities.

There are approximately 15 virally encoded proteins that participate in the assembly of the amorphous tegument structure, and these tegument proteins occupy the majority of the mass in the virion (18, 25, 40). The results demonstrated binding of VP8 to intron-less mRNA but not intron-containing mRNA of bICP0. Cells from such plaques produced infectious gD- virus, named gD-infBHV-1, which entered cells much more slowly than wild-type BHV-1. Since gB is essential for BHV-1 replication, only recombinant virions that have acquired a functional gB could give rise to infectious progeny. Calves latently infected with the 51g mutant did not reactivate from latency because virus shedding did not occur in ocular or nasal cavities. The tegument retains its structural integrity in the absence of the capsid and envelope, indicating strong intermolecular interactions that must exist between these tegument proteins to support the seemingly amorphous structure (7, 27, 40).

Inhibition of nuclear accumulation of STAT1 also occurred during BoHV-1 infection, while nuclear translocation of STAT1 was observed in BoHV1-ΔUL47-infected cells. This together with the observation that mutant VP8 is present in virions, albeit in lower amounts, suggests that the incorporation of VP8 may occur at two stages. C40UL3.5, when either transiently or stably expressed, inhibited αBTIF-mediated transactivation of a BoHV-1 immediate-early promoter. Mettenleiter, J. The mucosal explant models showed an intact 3D structure and contained all resident mucosal target cells and consequently is ideal to study the virus-host interactions at the site of infection. The experiment showed that after vaccination, BuHV-1 replication was significantly reduced by approximately three titer points compared to the controls.

AB – Serum and glucocorticoid-regulated protein kinases (SGK) are serine/threonine protein kinases that contain a catalytic domain resembling other protein kinases: AKT/protein kinase B, protein kinase A, and protein kinase C-Zeta for example. Collectively, this study provides insight into our understanding of early stages of BHV-1 infection. However, EHV-1 infected the monocytic cells (MC) and hijacked these cells to invade the lamina propria. Infection of cell cultures with the resulting gM(-) mutant of BHV-1/F(syn) led to formation of syncytia, whereas the CPE in gM(-)BHV-1 infected cells was comparable to the CPE in wtBHV-1 infected cultures. A thorough study of primary replication at both mucosae could elucidate whether or not different BoHV-1 subtypes show differences in mucosa tropism. The UL7 open reading frame encodes a protein of 300 amino acids with a calculated molecular mass of 32 kDa.

Nauwynck,* DVM, PhD, is a Full Professor in Virology and Director of the Laboratory of Virology, Department Virology, Parasitology and Immunology. We observed that, during wild-type BHV-1 infection, PGD2 levels were increased intracellularly and decreased in the medium. Since it has been shown that glycoprotein M (gM) of pseudorabies virus inhibits BRSV F-induced syncytium formation in transient plasmid transfection experiments [Pseudorbies virus glycoprotein M inhibits membrane fusion. The alphaherpesvirus UL47 gene encodes a protein that is assembled into the tegument of the virion (1, 7, 10, 23). Glycoprotein D (gD) of bovine herpesvirus 1 (BHV-1) has been shown to be an essential component of virions involved in virus entry. We previously reported that BHV-1 infection induces the activation of MAPK/Erk1/2 signaling in MDBK cells [16].

Replication-competent and replication-defective bovine adenovirus type 3 recombinants expressing the bovine herpesvirus type 1 (BHV-1) glycoprotein D (gD) were tested for induction of gD specific immune responses in calves using intratracheal (1st and 2nd immunization) and sub-cutaneous (3rd immunization) route of immunization. The UL47 gene product, VP8, is the most abundant tegument protein of bovine herpes virus-1 (BoHV-1). The immediate-early transactivator protein BICPO is a key regulatory element of bovine herpesvirus 1 (BHV-1) replication based on transient expression assays.