Antibody Response to Structural Proteins of Measles Virus in Patients With Natural Measles and Subacute Sclerosing Panencephalitis

Satô, Takeshi; Hayami, Masanori; Yamanouchi, Kazuya

doi:10.7883/yoken1952.34.365

Cited by 7 publications

(3 citation statements)

References 16 publications

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“…This observation has led to the hypothesis that SSPE is caused by a persistent infection of a measleslike defective virus in M protein which is responsible for the virus assembly. Similar results have been reported by others using the immunoprecipitation method (19,20,24,26,28). However, there are some conflicting reports from researchers using the same method (17,22) and also from those using other methods, i.e., solidphase radioimmunoassay (27) or immunoblotting (13).…”

supporting

confidence: 91%

Detection of Antibody to M Protein of Measles Virus in Patients with Subacute Sclerosing Panencephalitis: A Comparative Study on Immunoprecipitation

Ohara

Tashiro

Takase

et al. 1985

Microbiology and Immunology

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Consistent results have not been obtained yet on the presence of antibody to the M protein of measles virus in the sera of patients with subacute sclerosing panencephalitis (SSPE).We performed a comparative study on various immunoprecipitation systems which appeared in the literature and found that the difference in the composition of the solubilizing buffer produced a large variety of results on the immunoprecipitation.[35S] Methionine-labeled Vero cells infected with the Edmonston strain of measles virus were solubilized by 10 different buffers, and reacted with hyperimmune rabbit serum to whole virus, monospecific antisera to H, NP, and M proteins of the virus, normal adults' sera, and the sera from 16 SSPE patients .The immune complex was absorbed by protein A and both solubilization and precipitation rates were compared with each viral protein.Although viral proteins were solubilized by all buffers, the solubilization rate varied considerably . M protein was solubilized and was not coprecipitated nonspecifically with any of the other viral proteins.Purified protein A conjugated to Sepharose was preferable to Staphylococcus aureus for absorption of the immune complex since the latter absorbed both viral and host proteins nonspecifically. The precipitation rates of the viral proteins also varied according to the buffers.Better solubilization of the viral proteins seemed to reduce their rate of precipitation for which the presence of SDS may be responsible, and the presence of the protease inhibitors may also affect the results of immunoprecipitation.Detection of M protein in the immunoprecipitates was largely influenced by the kind of buffer used: some buffers could detect it clearly , but others could not defect it at all. Among the solubilizing buffers tested, Saleh's buffer (Virology 93: 369-376 (1979)), which contains 0.5% DOC and 0.5% Triton X-100, was most reliable for detection of the anti-M antibody in the rabbit serum, because it showed a high solubilization and high precipitation rates of viral proteins without nonspecific absorption by protein A or coprecipitation of M proteins with any of the other proteins.Using this buffer, we could definitely detect M proteins in the immunoprecipitates from the sera of all six healthy adults and 15 out of 16 patients with SSPE. It was found, however, that the amount of M proteins in SSPE patients was lower than that in healthy adults and varied considerably.

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confidence: 91%

Detection of Antibody to M Protein of Measles Virus in Patients with Subacute Sclerosing Panencephalitis: A Comparative Study on Immunoprecipitation

Ohara

Tashiro

Takase

et al. 1985

Microbiology and Immunology

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“…By immunoprecipitation we demonstrated that the antibody response to mumps virus was similar in the patient's serum and CSF and was directed against nearly all structural proteins including M-protein. In chronic measles-virus encephalitis a lack of antibodies against M-protein has been detected and the possibility of defective viral protein synthesis has been discussed, 26,27 The present case could represent a chronic form of mumps virus infection in the CNS. This can only be confirmed by virus isolation or demonstration of antigen within brain tissue.…”

Section: Discussionmentioning

confidence: 81%

Chronic Encephalomyelitis With Specific Increase in Intrathecal Mumps Antibodies

Vaheri

Julkunen

Koskiniemi³

1982

The Lancet

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Symptoms of severe encephalomyelitis developed in a 31-year-old man in 1967. He had a high serum antibody titre to mumps virus associated with a polymorphic cell reaction and an increased protein concentration in cerebrospinal fluid (CSF). He recovered considerably within a year and was able to resume work. In 1975 his condition deteriorated again; it improved during the following few years, but a further deterioration then occurred. In March, 1981, the complement-fixing antibody titre to mumps virus was 1/32 in the serum and 1/4 in the CSF. In November, 1981, the CSF IgG index was increased and the altered serum/CSF antibody ratio persisted. The specificity of the altered antibody ratio was confirmed by the single radial haemolysis test and an immunoassay specific for mumps virus. Antibodies against the mumps virus envelope glycoprotein, M-protein, and nucleoprotein could be demonstrated by immunoprecipitation and the antibody patterns in serum and CSF were similar. Antibodies against other microorganisms were not detected in the patient's CSF, and mumps antibodies were not found in the CSF specimens of 57 control patients. This case may be an example of a new disease-chronic mumps virus infection in the central nervous system.

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“…No band corresponding to the M protein was visualized from the immunoprecipitate using M A b s against the M protein, in accordance with the previous study (Sato et al, 1985) (data not shown). Monkey hyperimmune serum against MV and a convalescent serum from an atypical measles patient, both of which strongly react with all structural proteins of MV including the M protein (Sato et al, 1981(Sato et al, , 1988, gave rise to a faint, barely recognizable M protein band (data not shown). By contrast, the M protein band was clearly resolved after immunoprecipitation with anti-M serum from a rabbit immunized with the M protein prepared after separation by S D S -P A G E (Fig.…”

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confidence: 96%

Matrix Protein of Cell-associated Subacute Sclerosing Panencephalitis Viruses

Enami

Satô

Sugiura

1989

Journal of General Virology

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SUMMARYThe nucleotide sequence has been determined for the matrix (M) protein gene of three strains, Niigata-1, ZH and Biken, of cell-associated subacute sclerosing panencephalitis (SSPE) virus. The M proteins of the Niigata-1 and ZH strains were found to terminate prematurely as a result of nonsense mutations at nucleotide positions 68 and 96 respectively. On the other hand it was predicted that the Biken strain would express M protein with 22 amino acid differences and eight additional amino acids at its C terminus in comparison to the M protein of the Edmonston strain of measles virus. Radiolabelling of cells carrying the Biken strain showed the production of an M protein with considerably altered immunoreactivity and a marked reduction in intracellular stability. Either premature termination or rapid degradation of the M protein may underlie the defectiveness of these three strains of SSPE virus.

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Antibody Response to Structural Proteins of Measles Virus in Patients With Natural Measles and Subacute Sclerosing Panencephalitis

Cited by 7 publications

References 16 publications

Detection of Antibody to M Protein of Measles Virus in Patients with Subacute Sclerosing Panencephalitis: A Comparative Study on Immunoprecipitation

Detection of Antibody to M Protein of Measles Virus in Patients with Subacute Sclerosing Panencephalitis: A Comparative Study on Immunoprecipitation

Chronic Encephalomyelitis With Specific Increase in Intrathecal Mumps Antibodies

Matrix Protein of Cell-associated Subacute Sclerosing Panencephalitis Viruses

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