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Interference of measles virus (MV) with phosphatidyl-inositol-3-kinase (PI3K) activation in response to T cell receptor ligation was identified as important for the induction of T cell paralysis. We now show that MV exposure of unstimulated T cells induces expression of SIP110, an isoform of the
The influence of wild (Co-69) and attenuated (L-16) measles virus infection on the activity and activation energy of lactate dehydrogenase (LDH), acid and alkaline phosphatases (P-ase) was tested in R9CA monkey kidney cells at various time intervals after inoculation. With both virus strains
Dendritic cells (DCs) are targets of measles virus (MV) and play central roles in viral dissemination. However, DCs express the RIG-I-like receptors (RLRs) RIG-I and Mda5 that sense MV and induce type I interferon (IFN) production. Given the potency of this antiviral response, RLRs are tightly
The cytosolic sensor MDA5 is crucial for antiviral innate immune defense against various RNA viruses including measles virus; as such, many viruses have evolved strategies to antagonize the antiviral activity of MDA5. Here, we show that measles virus escapes MDA5 detection by targeting the
Human CD46, formerly membrane cofactor protein, binds and inactivates complement C3b and serves as a receptor for measles virus (MV), thereby protecting cells from homologous complement and sustaining systemic measles infection. Suppression of cell-mediated immunity, including down-regulation of
Measles virus (MeV) causes several unique syndromes, including transient immunosuppression. To clarify the cellular responses to MeV infection, we previously analyzed a MeV-infected epithelial cell line and a lymphoid cell line by microarray and showed that the expression of numerous genes was up-
During viral infection, RIG-I-like receptors (RLRs) are activated upon dephosphorylation by the phosphatase PP1, resulting in type I interferon production. In this issue, Davis et al. (2014) and Mesman et al. (2014) show that measles virus inhibits this antiviral response by targeting PP1 and thus
Measles virus nucleoprotein is the most abundant viral protein and tightly encapsidates viral genomic RNA to support viral transcription and replication. Major phosphorylation sites of nucleoprotein include the serine residues at locations 479 and 510. Minor phosphorylation residues have yet to be
In this work we characterized the infection of a primary culture of rat osteoblastic lineage cells (OBCs) with measles virus (MeV) and the effect of infection on cell differentiation and maturation. Infection of OBCs with MeV led to high titers of infectivity released early after infection. Also,
In 54 children aged 1.5-2 years, immunized with the same batch of live measles vaccine prepared from strain, the relative and absolute numbers of different lymphocyte subpopulations were determined in parallel by means of two cytochemical reactions: for acid alpha-naphthyl acetate esterase and acid
Enzyme-immunoassays using an indirect method with alkaline phosphatase conjugated antiglobulins were satisfactory for detection of antibody to Measles and Cytomegalovirus. The antigen was passively adsorbed to polystyrene micro-harmagglutination plates for the assays. IgM antibody to Rubella was
The subcellular distribution of the phospholipase activities and metabolism of lysophosphatidylcholine in cultured human cell line (FL cells) during "fusion-from-within" induced by measles virus were studied. During cell fusion, fairly high activities of phospholipase A1 and A2, the optimal pHs of