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At least 19 recordsLinked to original sources
PubMed1993

Dot immunobinding assay for simultaneous detection of specific immunoglobulin G antibodies to measles virus, mumps virus, and rubella virus.

A dot immunobinding assay was used to detect antibodies to measles virus, mumps virus, and rubella virus antigens. Filter paper soaked with serum or whole blood was directly applied to the antigen-coated nitrocellulose sheets. The test was easy to perform, and its results agreed very well with those obtained by standard enzyme immunoassay.

Antibodies, Viral↗
PubMed1971

Incorporation of radioactive seleno-(75Se)-methionine into mumps virus.

Mumps virus was grown in embryonated chicken eggs in the presence of radioactive seleno-((75)Se)-methionine. Virus in the allantoic and amniotic fluids was concentrated in a sucrose density gradient, and a peak of viral material coincided with a significant peak of (75)Se-radioactivity. The radioactivity was acid-insoluble and remained associated with the virus after purification by erythrocyte adsorption and elution and centrifugation on a second sucrose density gradient. After amino-acid hydrolysis of the radioactive virus, only (75)Se-methionine was recovered by chromatographic analysis. These results demonstrate that the radioactive (75)Se-methionine was incorporated into protein of infectious mumps virus.

Adsorption↗
PubMed1976

Polypeptides of mumps virus.

Mumps virus was propagated in the extra-embryonic fluids of embryonated chicken eggs and was labeled by cionjection of radioactively labeled amino acids. The virus was purified by density gradient centrifugation, and its polypeptides were analyzed by polyarylamide gel electrophoresis. The virus was found to be composed of six polypeptides, ranging in size from 40,000 to 64,000 daltons. Viral proteins 1 and 3 were the glycoproteins of the virons. When the virus particle was treated with noniontic detergents, a small fraction of these glycoproteins could be released into the supernatant. After treatment with nonionic detergents in high salt and alkaline conditions, more of the surface glycoproteins were removed. This treatment also released the smallest viral polypeptide from the virion. The glycoproteins were separated using an affinity chromatographic column of agarose-fetuin. The heavier glycoprotein, viral protein 1, was found to contain both the neuraminidase and hemagglutinating activity. The two glycoproteins were tested for their ability to react in complement-fixing tests with mumps antisera. Only the heavier glycoprotein reacted with antisera possessing both anti-S and anti-V activity. Neither glycoprotein reacted with antisera specific for the S antigen. Thus, it was concluded that this glycoprotein corresponds to the classical V antigen of mumps virus.

Animals↗
PubMed1994

Detection of immunoglobulin G to measles virus, rubella virus, and mumps virus in serum samples and in microquantities of whole blood dried on filter paper.

Immunity to measles virus, rubella virus, and mumps virus was determined by EIA in serum samples and in dried whole blood specimens spotted on Whatman filter paper (5 mm in diameter). Both specimens were obtained from each patient by venepuncture and finger prick. Ten microliters of whole blood is enough to detect antibodies to these three different viruses. The comparison of the results obtained by EIA from 227 serum and whole blood samples have demonstrated close agreement: 98.6% for measles virus, 99.1% for rubella virus, and 96.0% for mumps virus. Moreover, 96 whole blood samples can be tested in a microtiter plate and can be stored at room temperature for 15 days or at +4 degrees C for several months. Therefore, whole blood dried on filter paper is a convenient alternative method for collecting and transporting specimens, it is easier and safer than venepuncture, and could be used for large-scale epidemiological studies, especially in newborns. This method could solve the problem of sampling, especially in young children, and could simplify studies of vaccine efficacy.

Adult↗
PubMed1985

Chronic mumps virus encephalitis. Mumps antibody levels in cerebrospinal fluid.

To study the outcome of mumps virus encephalitis 47 patients were contacted 1-15 years after the acute encephalitis associated with mumps virus infection. Twenty-three patients experienced clinical sequelae such as difficulties in memory and learning, focal motor or sensory signs, and loss of hearing and visual acuity. Lumbar puncture was performed on 8 patients. Antibodies to mumps virus were detected in 6 cerebrospinal fluid (CSF) specimens using enzyme immunoassay and in 3 patients an abnormal serum/CSF antibody ratio was observed 11, 26 and 58 (controls greater than 85); 14.3, 1.4 and 6.1 years after the acute encephalitis, respectively. Antibodies to other microbes were either undetectable in the CSF or the serum/CSF ratios were normal. The clinical sequelae in about half of the patients and the signs of intrathecal mumps antibody production are suggestive of a chronic process in the central nervous system after encephalitis associated with mumps virus infection.

Adult↗
PubMed1991

Efficient induction of Semliki Forest virus and mumps virus neutralizing anti-anti-idiotypic antibodies using Quil A as adjuvant.

Rabbit anti-idiotypic sera were prepared against Semliki Forest virus (SFV) neutralizing monoclonal antibody (MAb) UM 1.13 and mumps virus neutralizing MAb UM 10B. From these sera anti-idiotypic antibodies were purified by ammonium sulphate precipitation and subsequent affinity column chromatography. Anti-iso- and anti-allotypic antibodies were removed by binding to normal mouse serum immunoglobulins coupled to CNBr activated Sepharose. Peak protein fractions eluted from columns loaded with homologous MAb were used for anti-anti-idiotypic immunization of BALB/c mice to raise virus neutralizing anti-anti-idiotypic antibodies. Two intracutaneous immunizations, five weeks apart, with affinity purified rabbit polyclonal anti-idiotypic antibody (40 micrograms protein per animal) coupled to keyhole limpet hemocyanin and mixed with the adjuvant Quil A (50 microliters per animal) were sufficient to evoke neutralizing antibodies against either virus. Moreover the mice who developed SFV neutralizing serum antibodies upon anti-idiotypic immunization all survived an otherwise lethal challenge with virulent SFV.

Adjuvants, Immunologic↗
PubMed1997

Comparison of the Vidas and Bio-Whittaker enzyme immunoassays for detecting IgG reactive with varicella-zoster virus and mumps virus.

A total of 215 sera, 164 positive and 51 negative for antibody reactive with varicella-zoster virus (VZV), were analyzed using two commercially available enzyme immunoassays (EIAs) for detecting VZV-IgG, the Vidas Varicella-Zoster IgG assay (bioMeriéux Vitek, Inc., Hazelwood, MO, USA) and the Bio-Whittaker Varicella II assay (Bio-Whittaker, Inc., Walkersville, MD). The sensitivity and specificity of the Vidas and EIA for VZV-IgG was 98.9 and 100%, respectively. The sensitivity of the Bio-Whittaker VZV-IgG EIA assay was 98.8%, specificity 96.1%. Equivocal results were obtained with 4 and 2 sera, respectively. A total of 185 sera, 169 positive and 16 negative for mumps virus antibody, were analyzed with Vidas and Bio-Whittaker mumps IgG EIAs. The sensitivity of the two assays for detecting mumps IgG was 99.4% and 95.7%, respectively. Both assays demonstrated 100% specificity. Two of the 185 sera tested for mumps antibody yielded equivocal results with the Vidas EIA; four equivocal results were obtained with the Bio-Whittaker EIA.

Antibodies, Viral↗
PubMed1984

Antibody responses to mumps virus proteins in natural mumps infection and after vaccination with live and inactivated mumps virus vaccines.

Paired sera from 20 patients with acute mumps infection, 16 from persons vaccinated with live attenuated mumps virus vaccine, and 12 from persons vaccinated with formalin-inactivated virus vaccine were studied for mumps antibodies by single radial hemolysis (SRH), hemagglutination inhibition (HI), and by enzyme immunoassays (EIA) specific for whole virus, envelope glycoprotein, and nucleocapsid antibodies. Mumps patients had diagnostic rises in serum mumps antibodies in 90-100% of the cases depending on the method of assay. Vaccination resulted in seroconversion in 75-88% (live vaccine) and in 92% (inactivated vaccine) of the cases as detected by SRH or EIAs, whereas HI detected seroconversion only in 38% and 58% of the cases, respectively. Immunoprecipitation analyses revealed that all sera from mumps patients and nearly all postvaccination sera had antibodies against the main structural proteins of mumps virus. By immunoblotting, antibodies against denatured hemagglutinin-neuraminidase (HN) and fusion protein (F) were detected in 15-25% of mumps patients and persons vaccinated with live vaccine, whereas most postvaccination sera from those vaccinated with inactivated vaccine had HN (92%) and F (83%) protein antibodies, suggesting that antibodies against the denatured form of proteins are formed.

Antibodies, Viral↗
PubMed1988

Molecular cloning and sequence analysis of the mumps virus gene encoding the P protein: mumps virus P gene is monocistronic.

The nucleotide sequence of the P (phosphoprotein) gene of two strains of mumps virus has been determined from overlapping cDNA clones. The P gene contained a single open reading frame coding for a protein of 391 amino acids with a calculated Mr of 41,587, in good agreement with the value (40K to 45K) estimated from electrophoretic mobility on SDS-polyacrylamide gels. No open reading frame analogous to the C gene of other paramyxoviruses existed in the mumps virus P gene region. Comparison of the amino acid sequence of the mumps virus P protein with that of Newcastle disease virus showed a limited sequence homology.

Amino Acid Sequence↗
PubMed1999

The mumps virus neurovirulence safety test in Rhesus monkeys: a comparison of mumps virus strains.

Wild type mumps viruses are highly neurotropic and a frequent cause of aseptic meningitis in unvaccinated humans. To test whether attenuated mumps viruses used in the manufacture of mumps vaccines have neurovirulent properties, a monkey neurovirulence safety test (MNVT) is performed. However, results with several mumps virus MNVTs have raised questions as to whether the test can reliably discriminate neurovirulent from nonneurovirulent mumps virus strains. Here, various mumps virus strains representing a wide range of neuropathogenicity were tested in a standardized MNVT. A trend of higher neurovirulence scores was observed in monkeys inoculated with wild type mumps virus versus vaccine strains, although differences were not statistically significant. Results indicated the need for further examination and refinement of the MNVT or for development of alternative MNVTs.

Animals↗
PubMed1981

Cellular source of interferon induced in human peripheral blood mononuclear leukocytes by mumps virus or by tumour cells persistently infected with mumps virus.

Human leukocyte interferon (IFN-a) was induced in cultures of human peripheral blood mononuclear leukocytes (PBML) from seropositive healthy donor infected by mumps virus, or by a human lung carcinoma cell line (Pc-10) persistently infected with mumps virus (Pc-10/M-V). Adherent cells (M0), non-T, non-B cells and B cells all produced IFN in response to mumps virus or Pc-10/MpV cells. The non-T, non-B cells co-cultured with Pc-10/MpV cells produced high-titred IFN. However, T cells did not produced any antiviral factors even in the presence of M0. Furthermore, T cells activated with phytohaemagglutinin (PHA-P), concanavalin A or treated with u.v.-irradiated mumps virus, or Pc-10/MpV cells pretreated with mitomycin C did not produce any antiviral factors in response to either mumps virus or Pc-10/MpV cells.

Carcinoma↗
PubMed1992

The haemagglutinin-neuraminidase glycoprotein of the porcine paramyxovirus LPMV: comparison with other paramyxoviruses revealed the closest relationship to simian virus 5 and mumps virus.

The complete nucleotide sequence of the haemagglutinin-neuraminidase (HN) gene of the porcine paramyxovirus LPMV, was determined from cDNA derived from viral genomic RNA. The gene was 1906 nucleotides long including a putative gene end and poly A signal. One long open reading frame was found encoding a protein of 576 amino acids with a calculated molecular weight of 63,324. The protein contains four potential N-glycosylation sites and a major hydrophobic region near the N-terminal, suggesting a membrane anchor domain. Comparison of the deduced amino acid sequence of the LPMV HN protein with that of other paramyxovirus HN proteins, revealed the highest amino acid identity to simian virus 5 of 43% and mumps virus of 41%.

Amino Acid Sequence↗