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PubMed2000

Consequences of Fas-mediated human dendritic cell apoptosis induced by measles virus.

Mortality from measles virus (MV) infection is caused mostly by secondary infections associated with a pronounced immunosuppression. Dendritic cells (DCs) represent a major target of MV and could be involved in immunosuppression. In this study, human monocyte-derived DCs were used to demonstrate that DC apoptosis in MV-infected DC-T-cell cocultures is Fas mediated, whereas apoptotic T cells could not be rescued by blocking the Fas pathway. Two novel consequences of DC apoptosis after MV infection were demonstrated. (i) Fas-mediated apoptosis of DCs facilitates MV release, while CD40 activation enhances MV replication in DCs. Indeed, detailed studies of infectious MV release and intracellular MV nucleoprotein (NP) showed that inhibition of CD40-CD40L ligand interaction blocks NP synthesis. We conclude that the CD40 ligand expressed by activated T cells first enhances MV replication in DCs, and then Fas ligand produced by activated T cells induces Fas-mediated apoptosis of DCs, thus facilitating MV release. (ii) Not only MV-infected DCs but also bystander uninfected DCs undergo a maturation process confirmed by CD1a, CD40, CD80, CD86, CD83, and major histocompatibility complex type II labeling. The bystander maturation effect results from contact and/or engulfment of MV-induced apoptotic DCs by uninfected DCs. A model is proposed to explain how both a specific immune response and immunosuppression can simultaneously occur after MV infection through Fas-mediated apoptosis and CD40 activation of DCs.

Apoptosis↗
PubMed2004

A target site for template-based design of measles virus entry inhibitors.

Measles virus (MV) constitutes a principal cause of worldwide mortality, accounting for almost 1 million deaths annually. Although a live-attenuated vaccine protects against MV, vaccination efficiency of young infants is low because of interference by maternal antibodies. Parental concerns about vaccination safety further contribute to waning herd immunity in developed countries, resulting in recent MV outbreaks. The development of novel antivirals that close the vaccination gap in infants and silence viral outbreaks is thus highly desirable. We previously identified a microdomain in the MV fusion protein (F protein) that is structurally conserved in the paramyxovirus family and constitutes a promising target site for rationally designed antivirals. Here we report the template-based development of a small-molecule MV inhibitor, providing proof-of-concept for our approach. This lead compound specifically inhibits fusion and spread of live MV and MV glycoprotein-induced membrane fusion. The inhibitor induces negligible cytotoxicity and does not interfere with receptor binding or F protein biosynthesis or transport but prevents F protein-induced lipid mixing. Mutations in the postulated target site alter viral sensitivity to inhibition. In silico docking of the compound in this microdomain suggests a binding model that is experimentally corroborated by a structure-activity analysis of the compound and the inhibition profile of mutated F proteins. A second-generation compound designed on the basis of the interaction model shows a 200-fold increase in antiviral activity, creating the basis for novel MV therapeutics. This template-based design approach for MV may be applicable to other clinically relevant members of the paramyxovirus family.

Animals↗
PubMed1991

Use of immunofluorescence to identify measles virus infections.

Monoclonal antibody to measles virus was used successfully to identify measles virus antigen directly in clinical specimens, as well as in cell cultures. Pooled nasopharyngeal-throat swab specimens had a higher yield than throat swabs or urine samples for virus detection. Use of A549 cell cultures in the spin amplification vial assay proved to be highly efficient, allowing virus recognition within 1 to 2 days of inoculation. A combination of appropriately collected specimens, which includes a nasopharyngeal-throat swab, direct antigen detection with monoclonal antibody to measles in an indirect immunofluorescence system, and the spin amplification vial assay using A549 cells provides a sensitive and rapid system for isolation and/or identification of measles virus infections.

Antibodies, Monoclonal↗
PubMed1991

Viral RNA species in cell lines persistently and lytically infected with measles virus.

Identical measles viral mRNA species were present in similar amounts in the persistently infected cell lines LU106, HEpPi and MaSSPE, and in lytically infected cells as determined from Northern blots. The attenuation of transcription with the gene order did not vary significantly between different infected systems. A previously described selective restriction of F protein production in Lu106 cells could not be explained by defective transcription of F mRNA. RNA synthesis also continued unimpeded at restrictive temperatures for the temperature-sensitive viruses in Lu106 and HEpPi cells. Northern blotting revealed a prominent band in HEpPi RNA and a weak band in Lu106 RNA with the characteristics of incomplete genomes. In all infected cells, previously unrecognized small RNA species, hybridizing with the F- and H-specific probes, were discovered.

Animals↗
PubMed2004

The 12 A structure of trypsin-treated measles virus N-RNA.

Recombinant measles virus nucleoprotein (N) was produced in insect cells where it bound to cellular RNA to form helical N-RNA structures. These structures were observed by electron microscopy but were too flexible for high-resolution image analysis. Removal of the C-terminal tail of N by trypsin treatment resulted in structures that were much more rigid and seemed more regular. Several methods of image analysis were employed in order to make a helical reconstruction of the digested N-RNA. During this analysis, it became clear that the apparently regular coils of digested N-RNA consisted of a series of closely related helical states. The iterative helical real space reconstruction method allowed the identification of two helical states for which a reconstruction could be calculated. The model with the highest resolution shows N monomers that consist of three domains and that are connected to their neighbours by two narrow connections, one close to the helical axis and another toward the middle of the monomers. There are no connections between N molecules in subsequent helical turns. After labelling the RNA in the structure with cis-platinum, the connection closest to the helical axis increased in density, suggesting the position of the RNA. The shapes of the monomers of the nucleoproteins of influenza virus, rabies virus (both determined before) and that of measles virus (determined here) are all similar, whereas the overall shapes of their respective N-RNAs (nucleocapsids) is very different. This is probably due to the position and number of the connections between the N subunits in the N-RNA, one for influenza virus allowing much flexibility, two for rabies virus at either end of the N molecules leading to ribbons and two for measles virus leading to the typical paramyxovirus helical nucleocapsid.

Amino Acid Sequence↗
PubMed1998

Molecular cloning of membrane cofactor protein (MCP; CD46) on B95a cell, an Epstein-Barr virus-transformed marmoset B cell line: B95a-MCP is susceptible to infection by the CAM, but not the Nagahata strain of the measles virus.

Measles virus (MV) infects not only human beings but also some simian species. The MV receptor on Vero cells (a cell line established from African Green monkey kidney cells) and human cells has been shown to be the membrane cofactor protein MCP/CD46, which is an inhibitor of autologous complement (C) activation. B95a, an Epstein-Barr virus (EBV)-transformed marmoset B cell line, is a simian cell line used for MV selection and is much more susceptible to MV than Vero cells. In the present study, we isolated cDNAs encoding MCP homologues from B95a cDNA library and assessed whether B95a-MCP is responsible for the high susceptibility of B95a to MV. The deduced amino acid sequence of the cDNA of B95a-MCP was 76% identical to that of human-MCP, and the recombinant B95a-MCP exerts C inhibitor activity. Although CAM, a vaccine strain of MV, infected Chinese hamster ovary (CHO) cells expressing B95a-MCP, Nagahata strain, a wild type of MV, failed to infect the CHO transfectants, suggesting that additional membrane molecules of B95a are responsible for the high susceptibility of B95a to the Nagahata strain.

Amino Acid Sequence↗
PubMed1976

Growth of measles virus in nervous tissues. IV. Neurovirulence of wild measles and SSPE viruses in monkeys.

Neurovirulence of in vivo-passed wild measles virus and that of the cell-associated SSPE virus were compared by intracerebral inoculation into monkeys. The wild measles virus was found to lack neutrovirulence without producing neurological signs or significant histological changes in the brains, whereas the virus was confirmed to preserve the properties characteristic of the wild virus. In contrast, inoculation of the SSPE virus induced rapid onset of neurological signs with mild but definite histological changes including degeneration of nerve cells. The fact that SSPE virus exhibited neurovirulence in monkeys indicated importance of the current assay system for neurovirulence of measles vaccine by intracerebral inoculation into monkeys.

Animals↗
PubMed2001

Hemadsorption expressed by cloned H genes from subacute sclerosing panencephalitis (SSPE) viruses and their possible progenitor measles viruses isolated in Osaka, Japan.

Most subacute sclerosing panencephalitis (SSPE) viruses, including our Osaka-1, -2, and -3 strains isolated in Osaka, have shown negative hemadsorption (HAD) by African green monkey red blood cells. This property has been thought to be characteristic of SSPE virus as compared to the positive reaction of the standard Edmonston strain of measles virus (MV). However, this assumption has become quite obscure because MV mutates frequently at the genetic level during its multiplication and also because recent field strains isolated by lymphoblastoid cell lines have shown negative HAD. To investigate the above issue, the nucleotide sequences of the hemagglutinin (H) genes from SSPE virus Osaka-1, -2, or -3 strains were compared to those of various MV field strains isolated in Osaka by Vero cells. The H gene sequences of three SSPE strains were relatively conserved without such biased hypermutation as had been observed in the matrix (M) gene of three SSPE strains. However, this analysis of the H gene sequence of the SSPE viruses enabled us to deduce possible progenitor MVs, which are in agreement with the deduction from the M gene analysis we reported previously. The HAD of Vero cells transfected with the cloned H cDNAs from the SSPE strains and their progenitors suggested that negative HAD of the SSPE viruses has been maintained as one of original properties of the progenitor MVs rather than having been acquired as an altered one during long-term persistent infection in the brains of patients with SSPE.

Amino Acid Sequence↗
PubMed1988

Mice immunized with measles virus develop antibodies to a cell surface receptor for binding virus.

Mice were immunized with measles virus to determine whether an auto-anti-idiotypic antireceptor response could be generated as a probe for measles virus receptors. Mice initially responded to viral antigens (days 11 to 18) and subsequently developed antibodies to a putative measles virus receptor (peak at day 30 to 35) by three criteria: the sera (1) agglutinated erythrocytes which virus agglutinates, (2) reacted with Vero cells, and (3) inhibited virus attachment to Vero cells. Additionally, select sera inhibited virus infection of Vero cells. The cell-reactive activity was identified as immunoglobulin G antibody and was neutralized by sera reacting with virus (idiotype). The application of this anti-idiotypic antibody to identify measles virus-binding sites on Vero cells was revealed by the ability of sera to immunoprecipitate 20- and 30.5-kilodalton proteins from metabolically labeled ([35S]methionine) Vero cells.

Animals↗
PubMed1969

Electron microscopy of measles virus replication.

Replication of measles virus in HeLa cells was examined by electron microscopy with ultrathin sectioning and phosphotungstic acid negative staining methods. The cytoplasmic inclusion bodies consisted of masses of helical nucleocapsid which was similar in structure to the nucleocapsid found in measles virions. The cytoplasmic helical nucleocapsid appeared to align near the HeLa cell membrane, and the membrane differentiated into the internal membrane of the viral envelope and the outer layer of the short projections. The viral particles were released by a budding process involving incorporation into the viral envelope of membrane which was contiguous to but morphologically altered from the membrane of the HeLa cells. The intranuclear inclusion bodies were composed of tubular structures similar to those found in the cytoplasmic inclusion bodies. These structures aggregated to crystalline arrangement. The relationship between nuclear inclusion body and replication of measles virus was not clear.

Cell Membrane↗
PubMed1976

Some characteristics of salt-dependent haemagglutinating measles viruses.

Several strains of measles virus which did not agglutinate monkey erythrocytes in phosphate-buffered saline did so in buffer containing 0-8 M-ammonium sulphate. Haemadsorption to cells infected with these viruses was also salt-dependent. In a series of tests salt-dependent agglutinin was shown to be a stable structural component of the infectious virion. The relevance of these findings is discussed in the light of previous reports that many measles virus preparations do not agglutinate erythrocytes.

Ammonium Sulfate↗
PubMed1996

Immunization of mice with plasmid DNA expressing the measles virus nucleoprotein gene.

The measles virus (MV) nucleocapsid (N) protein gene has been inserted into a plasmid vector so as to place the gene under the control of the strong constitutive human cytomegalovirus major immediate early promoter. On intramuscular injection of pMV64 DNA into C3H/He mice, seroconversion with increasing titers of N-specific serum IgG antibodies was observed over a period of 3 months. However, when 3-week-old mice were immunized by intramuscular injection of pMV64 in a two-dose schedule, and challenged intracranially with a rodent-adapted measles virus strain (CAM/RB) at 5 weeks of age, no significant protective response was seen. The lack of effective protection evoked by DNA immunization in this model, where MV challenge must take place before 8 weeks of age, may be due to inefficient induction of cell-mediated immunity resulting from expression in muscle tissue, compounded by a relatively slow rise in immune response compared with that seen with the recombinant adenovirus.

Animals↗
PubMed2003

Update on the global distribution of genotypes of wild type measles viruses.

Molecular characterization of measles viruses is an important component of measles surveillance because these studies enhance our ability to identify the source and transmission pathways of the virus. Molecular surveillance is most beneficial when it is possible to observe the change in virus genotypes over time in a particular region. Such information can help to document the interruption of transmission of measles virus and thus provide an important method for assessing the effectiveness of vaccination programs. It is recommended that virus surveillance be conducted during all phases of measles control and be expanded to give an accurate description of the global distribution of measles genotypes. This review provides updated information on the circulation patterns of measles genotypes and examples of the utility of virologic surveillance.

Genetic Variation↗
PubMed1977

The effect of cycloheximide on the replication of measles virus.

Treatment of measles virus-infected cells with cycloheximide results in a three-fold increase of 3H-uridine incorporation into the 12 to 36S mRNA species and in the inhibition of genomic 50S RNA synthesis. Consistent with these observations was the finding of a build-up of polyribosomes but an absence of nucleocapsids in the infected cells. These results suggest that measles virus RNA replication, but not transcription, is dependent upon active protein synthesis.

Capsid↗
PubMed1982

Virus antibodies in Parkinson's disease. Herpes simplex and measles virus antibodies in serum and CSF and their relation to HLA types.

Serum and cerebrospinal fluid (CFS) immunoglobulin G (IgG) antibodies to herpes simplex (HSV) and measles viruses were assayed with a radioimmunoassay in 56 patients with idiopathic Parkinson's disease and in a similar number of age- and sex-matched controls with other neurological diseases. As a group, the patients with Parkinson's disease had a significantly increased serum antibody level against HSV, but measles virus antibody levels were similar in both groups. Both in the Parkinson's group and in the control group, the levels of the total IgG in CSF were within normal limits and the CSF antibodies to HSV and measles virus paralleled the serum antibody titers relative to the total IgG serum-to-CSF ratios. This indicates no increased intrathecal antibody production in either group. In 48 patients with Parkinson's disease who were HLA-typed, no association of viral antibody levels with particular HLS antigens were noted. The findings suggest that HSV is not present within the central nervous system of the patients with Parkinson's disease. The increase HSV antibody level seen in Parkinson's disease patients may reflect a more general disturbance of the patients' immune functions.

Adult↗
PubMed2003

Evaluation of serological and virological tests in the diagnosis of clinical and subclinical measles virus infections during an outbreak of measles in The Netherlands.

We evaluated different approaches for diagnosing measles virus (MV) infection in unvaccinated children and in healthy contact persons (n=194) during a measles epidemic in The Netherlands. MV RNA was detected by reverse-transcriptase polymerase chain reaction in throat-swab specimens from 93% of the patients with clinical symptoms. MV RNA was detected from 5 days before until 12 days after the onset of symptoms. Most patients (88%) also secreted MV RNA in their urine until 5 weeks after the onset of symptoms. Oral fluid proved to be the most practical specimen for the simultaneous detection of MV-specific IgM antibody and viral RNA, which, together, confirmed 93% of measles cases. Viral RNA was also detected in oropharyngeal specimens from 3 healthy contact persons with serological proof of MV infection. The results of this study emphasize the feasibility of combined detection of viral RNA and MV-specific IgM antibodies in oropharyngeal specimens for the diagnosis of clinical and subclinical MV infection.

Adolescent↗
PubMed1979

Transmembrane communication in cells chronically infected with measles virus.

The transmembrane association of the measles virus hemagglutinin and hemolysin surface proteins with intracellular viral antigens was studied. Rabbit antisera monospecific for measles virus matrix and nucleocapsid proteins and a human antiserum containing specificities for both the hemagglutinin and hemolysin proteins were used to study the co-capping of these proteins in human Lu 106 cell-line, chronically infected with measles virus. Capping of the surface-associated envelope components was accompanied by co-capping of the matrix and nucleocapsid proteins, the latter being localized mainly within the inclusions. This demonstrated transmembrane communication between surface-associated envelope components and the intracellular measles virus matrix and nucleocapsid proteins. The results demonstrated the existence of a linkage between viral inclusions and viral proteins associated with cell membranes. In the presence of cytochalasin B (1--2 micrograms/ml), co-capping of the matrix protein was unchanged or slightly enhanced, whereas co-capping of the nucleocapsid protein decreased, indicating that actin filaments may mediate the communication between viral nucleocapsids and the cell membrane.

Antigens, Surface↗