Detection of antibodies to individual proteins of rubella virus

Loo, Tip W.; Macdonald, Iain; Clarke, David M.; Trudel, Michel; Tingle, Aubrey J.; Gilam, Shirley

doi:10.1016/0166-0934(86)90083-2

Cited by 15 publications

(10 citation statements)

References 14 publications

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“…protein or RV. Mouse and rabbit antisera had previously shown to be RV specific, as judged by both ELISA and immunoprecipitation (27). Peptides Cl, C3, and C5 reacted strongly with the mouse antisera (Fig.…”

Section: Selection Of Peptidesmentioning

confidence: 74%

Analysis of T- and B-cell epitopes of capsid protein of rubella virus by using synthetic peptides

Ou¹,

Chong²,

Tripet³

et al. 1992

J Virol

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A nested set of 11 overlapping synthetic peptides covering the entire sequence of rubella virus capsid protein was synthesized, purified, and tested against human rubella virus-specific T-cell lines and rubella virusseropositive sera. T-cell lines derived from four donors responded strongly to four synthetic peptides containing residues 96 to 123, 119 to 152, 205 to 233, and 255 to 280. Only one peptide (residues 255 to 280) was recognized by all four T-cell lines. Two human immunodominant linear B-cell epitopes were mapped to residues 1 to 30 and 96 to 123 by using peptide-specific enzyme-linked immunosorbent assay. All 11 synthetic peptides were highly immunogenic and induced strong antibody responses in rabbits against the respective immunized peptides. Seven of the 11 rabbit antipeptide antisera (anti-1-30,-74-100,-96-123,-119-152,-205-233,-231-257, and-255-280) specifically recognized the capsid protein on immunoblots. Identification of these Tand B-cell epitopes represents the first step toward rational design of synthetic vaccines against rubella.

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Section: Selection Of Peptidesmentioning

confidence: 74%

Analysis of T- and B-cell epitopes of capsid protein of rubella virus by using synthetic peptides

Ou¹,

Chong²,

Tripet³

et al. 1992

J Virol

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“…Katow and Sugiura (19) demonstrated that although antibodies to El were predominant following most RV infections, anti-E2 antibodies were relatively more abundant following congenital infection. We have also observed abnormal distributions of anti-El, -E2, and -C reactivities in RV hemagglutination inhibitionor ELISA-seronegative individuals developing arthritis in close temporal association with RV infection or immunization (26,38), suggesting that previous RV exposure was associated with a failure to develop or sustain functional immunity. Similar dissociations between seroconversion and development of effective immunity to RV have been reported by others (15,18,36), indicating a need for a more sensitive and specific method of serodiagnosis.…”

mentioning

confidence: 66%

Detection of rubella virus-specific immunoglobulin G (IgG), IgM, and IgA antibodies by immunoblot assays

et al. 1992

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Immunoblot (IB) assays were developed for detection of rubella virus (RV)-specific immunoglobulin G (IgG), IgM, and IgA antibodies in human serum following natural infection or immunization. IB assays performed under nonreducing conditions were compared with those performed under reducing conditions and with immunoprecipitation assays. Significant loss of antigenicity (greater than 90%) of RV E1 and E2 proteins was observed when IB assays were performed in the presence of 2-mercaptoethanol as compared with assays under nonreducing conditions. In contrast, the antigenicity of RV capsid protein was not influenced by reducing agents. Sensitivity of IB for RV-specific IgG antibodies was determined to be 0.01 IU/ml under nonreducing conditions. In the determination of RV-specific IgM and IgA antibodies by IB, pretreatment of serum with protein G to remove competing high-affinity RV-specific IgG or rheumatoid factor significantly improved assay sensitivity. IB assays were observed to be superior to immunoprecipitation assays in their ability to better define the specificities of RV-specific antibodies and to detect antibodies of all immunoglobulin classes. However, the conformational sensitivity of RV protein antigenicity should be an important consideration in the interpretation of RV-specific antibodies by IB assays.

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“…The use of monoclonal antibodies (MAbs) has allowed the extensive study of different epitopes on these proteins. The targets of MAbs with hemagglutination-inhibition (HI) or neutralizing (NT) activity or both are located on the E1 protein [11][12][13] and a MAb specific for the E2 glycoprotein, with only NT activity, was also selected [11,14].…”

Section: Introductionmentioning

confidence: 99%

Immune responses to wild and vaccine rubella viruses after rubella vaccination

Cusi

Metelli

Valensin

1989

Archives of Virology

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Antibody responses to individual structural proteins (E1, E2, and C) of the M33 wild rubella virus and the RA 27/3 live attenuated rubella strain were assayed by immunoblotting in 11 girls, following immunization with RA 27/3 rubella vaccine. Serum samples were drawn before immunization and at 10 days, 1 month, 1 year, 2 years, and 3 years afterwards. All the subjects showed antibodies to E1 glycoprotein of both the virus strains up to three years after immunization, indicating the importance of E1 in immunity. Antibodies to E1 were always present when with neutralizing activity was observed. Antibodies to E2 protein of both the viruses and to the C protein of the M33 virus gradually disappeared with time in some samples, while antibodies to C protein of the RA 27/3 virus strain were found persistently in all the sera.

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Detection of antibodies to individual proteins of rubella virus

Cited by 15 publications

References 14 publications

Analysis of T- and B-cell epitopes of capsid protein of rubella virus by using synthetic peptides

Analysis of T- and B-cell epitopes of capsid protein of rubella virus by using synthetic peptides

Detection of rubella virus-specific immunoglobulin G (IgG), IgM, and IgA antibodies by immunoblot assays

Immune responses to wild and vaccine rubella viruses after rubella vaccination

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