Disease relevance of Semliki Forest Virus

• Using in vitro immunization, we have reconstructed three consecutive steps of an idiotype network to show that the nucleocapsid of Semliki Forest virus contains a specific 'receptor' for the cytoplasmic tail of the E2 spike glycoprotein [1].
• The Semliki Forest virus capsid protein contains a chymotrypsin-like protease domain that must fold before it can autocatalytically cleave the protein from a larger polyprotein precursor [2].
• Bafilomycin A1 (Baf), a specific inhibitor of the vacuolar-type proton pump, inhibited the entry of Semliki Forest virus and vesicular stomatitis virus into BHK-21 cells [3].
• We determined the subcellular localization of the GTPases by expressing the c-myc epitope-tagged proteins with the Semliki Forest virus and the vaccinia T7 vector systems [4].
• The alphavirus Semliki Forest virus (SFV) infects cells via a low-pH-dependent membrane fusion reaction mediated by the E1 envelope protein [5].

High impact information on Semliki Forest Virus

• Replicative form of Semliki Forest virus RNA contains an unpaired guanosine [6].
• PrP co-localizes with LRP/LR on the surface of N2a cells and Semliki Forest virus (SFV) RNA transfected BHK cells [7].
• In order to evaluate the role of this layer in different kinetic components of secretion, we used the Semliki Forest virus (SFV) system to infect adrenal chromaffin cells with SNAP-25 Q174L, a point mutant in the zero layer [8].
• Wild-type and mutant versions of human APP were expressed in hippocampal neurons using the Semliki forest virus system [9].
• We have compared the behavior of wild-type mouse NEDD-2, a neural precursor cell-expressed, developmentally down-regulated cysteine protease gene, to various mutant forms of the gene in both apoptotic activity in neuronal cells and proteolytic cleavage in the Semliki Forest virus and rabbit reticulocyte protein expression systems [10].

Chemical compound and disease context of Semliki Forest Virus

• Cholesterol is required for infection by Semliki Forest virus [11].
• This paper presents a kinetic analysis of low-pH-induced fusion of Semliki Forest virus (SFV) with cholesterol-containing unilamellar lipid vesicles (liposomes), consisting otherwise of phosphatidylcholine, phosphatidylethanolamine and sphingomyelin [12].
• These compartments were identified using Baby hamster kidney (BHK) cells infected with Semliki Forest virus (SFV) and treated with monensin [13].
• In this work we show that the p62 protein of Semliki Forest virus contains an uncleaved signal sequence at its NH2-terminus and that this becomes glycosylated early during synthesis and translocation of the p62 polypeptide [14].
• The effect of colchicine and dibucaine on the morphogenesis of Semliki Forest virus [15].

Biological context of Semliki Forest Virus

• Membrane fusion of Semliki Forest virus in a model system: correlation between fusion kinetics and structural changes in the envelope glycoprotein [12].
• Here we have completed mapping of the individual phosphorylation sites on Semliki Forest virus nsP3 (482 amino acids) by point mutational analysis of threonine residues [16].
• We have applied this sequencing procedure to verify the amino acid sequence deduced from the 26S RNA of Semliki Forest virus [17].
• A procedure to verify an amino acid sequence which has been derived from a nucleotide sequence: application to the 26S RNA of Semliki Forest virus [17].
• We report here the isolation of additional variants of both SIN and Semliki Forest virus (SFV) replicons encoding the neomycin resistance gene that can establish persistent replication in BHK cells [18].

Anatomical context of Semliki Forest Virus

• Dissection of the Golgi complex. I. Monensin inhibits the transport of viral membrane proteins from medial to trans Golgi cisternae in baby hamster kidney cells infected with Semliki Forest virus [19].
• Dissection of Semliki Forest virus glycoprotein delivery from the trans-Golgi network to the cell surface in permeabilized BHK cells [20].
• Using [14C]palmitoyl-CoA as donor and deacylated (fatty acid-free) structural proteins of Semliki Forest virus as exogenous acceptors, palmitic acid was incorporated into polypeptide in a cell-free system with microsomes of baby hamster kidney cells, chicken embryo fibroblasts, and rat liver cells [21].
• To address these issues, we examined the generation of both intracellular and secreted Abeta-(1-40) and Abeta-(1-42) in human neuronal NT2N cells, in primary rat astrocytes, and in Chinese hamster ovary cells engineered to express wild-type APP or APPDeltaNL using a recombinant Semliki Forest virus expression system [22].
• Chemical cross-linking of proteins of Semliki Forest virus: virus particles and plasma membranes from BHK-21 cells treated with colchicine or dibucaine [23].

Gene context of Semliki Forest Virus

• (iii) Reconstituted HLA-A and HLA-B vesicles interact in solution with Semliki Forest virus (or with vesicles containing viral spike proteins), as demonstrated by coprecipitation with antisera [24].
• The proteins coded for by the HLA-A and HLA-B loci in man and the H-2K and H-2D loci in mice were identified as cell surface receptors for Semliki Forest virus [24].
• As compared with APP-WT (primary neurons from control or PS1-deficient mice infected with Semliki Forest virus), PS1-/- neurons and PS1+/+ neurons overexpressing APP-Deltact (a slow-internalizing mutant) show a decrease of all secreted Abeta peptide species, as expected, because this mutant is processed mainly by alpha-secretase [25].
• As such, the current study presents a new delivery system that can simultaneously express three anti-tumor genes using a Semliki Forest virus (SFV) vector in the expectation of combined or synergistic effects of angiogenesis inhibition by angiostatin and apoptosis induction by p53, PTEN and the rSFV particle itself [26].
• This report describes the construction, characterization and the in vivo immunotherapeutic potential of recombinant Semliki Forest virus (SFV) expressing the HPV16 E6 and E7 proteins (SFV-E6E7) [27].

Analytical, diagnostic and therapeutic context of Semliki Forest Virus

• The nonstructural (ns) proteins nsP1 to -4, the components of Semliki Forest virus (SFV) RNA polymerase, were localized in infected cells by confocal microscopy using double labeling with specific antisera against the individual ns proteins [28].
• The dissociation of Semliki Forest virus induced by increasing concentrations of the anionic detergent sodium dodecyl sulfate was studied using density gradient centrifugation [29].
• Sequence analysis of lactosamine type glycans of individual membrane proteins of Semliki Forest virus [30].
• Immunoelectron microscopy was used to detect actin in wild-type (wt) Moloney murine leukemia virus (MoMuLV) and in virus-like particles (VLP) produced by recombinant Semliki Forest virus expressing only the MoMuLV gag polyprotein [31].
• Plaque assays of infected 6-16-/- cells showed that expression of the 6-16 gene was not required for the induction by interferon of an antiviral state against encephalomyocarditis virus, semliki forest virus or cocal virus [32].

References