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measles/phosphatase
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Measles virus induces expression of SIP110, a constitutively membrane clustered lipid phosphatase, which inhibits T cell proliferation.
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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
Activity of lactate dehydrogenase, acid and alkaline phosphatases in measles virus-infected monkey kidney cell cultures.
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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
Measles virus suppresses RIG-I-like receptor activation in dendritic cells via DC-SIGN-mediated inhibition of PP1 phosphatases.
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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
Antagonism of the phosphatase PP1 by the measles virus V protein is required for innate immune escape of MDA5.
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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
Functional modulation of human macrophages through CD46 (measles virus receptor): production of IL-12 p40 and nitric oxide in association with recruitment of protein-tyrosine phosphatase SHP-1 to CD46.
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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 Infection Inactivates Cellular Protein Phosphatase 5 with Consequent Suppression of Sp1 and c-Myc Activities.
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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-
[Effect of immunization against pertussis, measles and smallpox on the alkaline phosphatase of leukocytes].
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The effect of vaccination against measles on the white blood picture and the alkaline phosphatase activity of neutrophil leukocytes.
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[Alkaline phosphatase of leukocytes in measles].
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Measles virus takes a two-pronged attack on PP1.
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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
Newly identified minor phosphorylation site threonine-279 of measles virus nucleoprotein is a prerequisite for nucleocapsid formation.
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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
Experimental in vitro infection of rat osteoblasts with measles virus stimulates osteogenic differentiation.
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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,
[The cytochemical marking of lymphocyte subpopulations in determining the immunoreactivity status of children vaccinated with a live measles vaccine].
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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 for antibodies in measles, cytomegalovirus infections and after rubella vaccination.
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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
Release of lysosomal phospholipase A1 and A2 into cytosol and rapid turnover of newly-formed lysophosphatidylcholine in FL cells during fusion-from-within induced by measles virus.
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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
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