1996
DOI: 10.1128/jcm.34.9.2210-2218.1996
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Rubella reimmunization: comparative analysis of the immunoglobulin G response to rubella virus vaccine in previously seronegative and seropositive individuals

Abstract: Rubella virus (RV)-specific immunoglobulin G (IgG) antibodies were studied in military recruits undergoing unselected immunization with live attenuated measles, mumps, and rubella virus (MMR) vaccine. Three different whole-RV enzyme immunoassays (EIAs) and an epitope-specific EIA with a synthetic peptide (BCH-178c) representing a neutralization domain on the RV E1 envelope protein were used. Before vaccination, 84.2, 87.7, and 84.5% of the subjects tested (n ‫؍‬ 399) were found to be seropositive (>10 IU/ml or… Show more

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Cited by 24 publications
(5 citation statements)
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“…In contrast to the immunodominant E1 glycoprotein, antibodies to E2 have limited neutralizing activity and E2 lacks the ability to elicit antibodies that inhibit hemagglutination. [ 7 , 8 , 9 , 10 , 11 , 12 ] While antibodies to E1 are functional in virus neutralization by hampering virus attachment/cell entry and E1 conformational changes/trimerization during cell entry, the neutralization mechanism of anti-E2 antibodies remains largely unknown. [ 48 ] Glycoprotein E2 function warrants additional studies, but this protein is likely involved in conformational changes during virus entry and maturation, E1 activation, E1 trafficking, and virus membrane budding.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…In contrast to the immunodominant E1 glycoprotein, antibodies to E2 have limited neutralizing activity and E2 lacks the ability to elicit antibodies that inhibit hemagglutination. [ 7 , 8 , 9 , 10 , 11 , 12 ] While antibodies to E1 are functional in virus neutralization by hampering virus attachment/cell entry and E1 conformational changes/trimerization during cell entry, the neutralization mechanism of anti-E2 antibodies remains largely unknown. [ 48 ] Glycoprotein E2 function warrants additional studies, but this protein is likely involved in conformational changes during virus entry and maturation, E1 activation, E1 trafficking, and virus membrane budding.…”
Section: Resultsmentioning
confidence: 99%
“…[ 6 ] The E1 protein, in particular, is considered to be the immunodominant and hemagglutation-eliciting antigen that predominantly contributes to protective immunity. [ 7 , 8 , 9 , 10 , 11 , 12 ] Assays such as whole- rubella virus, recombinant protein and synthetic peptide-based enzyme immunoassays (including immunoblot), hemagglutination inhibition assays, and neutralization assays (including a high-throughput immunocolorimetric-based neutralization assay) have been used in large studies for surveillance of rubella vaccine-induced immunity. [ 13 , 14 , 15 , 16 , 17 , 18 , 19 , 20 ] Recent papers and expert reviews from the literature point to the lack of standardization of the international rubella antibody standard and the currently used commercial anti-rubella IgG antibody (Ab) assays (leading to misinterpretation of results), and recommend improved and/or alternative approaches in rubella serology testing (including qualitative testing and/or testing without the use of the existing RUBI-1-94 international rubella Ab standard for calibration of assays).…”
Section: Introductionmentioning
confidence: 99%
“…Immunity against rubella is directed against the E1 protein with neutralizing antibody titres most accurately correlating with protection from infection. However, SNA titres are less commonly measured than for measles; thus, binding IgG measured by enzyme-linked immunoassay (EIA) are also used to assess levels of rubella-specific immunity [36][37][38][39]. Furthermore, as with measles, although genotypic variation exists, these are not associated with antigenic differences in key epitopes; thus, only a single serotype consistently susceptible to vaccineinduced neutralizing antibodies has been identified [24].…”
Section: Rubellamentioning
confidence: 99%
“…The E1 and E2 rubella protein spikes are anchored to the external layer of the membrane, with membrane-bound E2 proteins bridging rows of E1 proteins, considered as the main immunodominant antigens responsible for controlling receptor-mediated endocytosis (Petruzziello et al, 1996;Katow and Sugiura, 1985). Antibody levels against the neutralizing domain of E1 correlate with protection against rubella virus (Mitchell et al, 1996;Cordoba et al, 2000;Wilson et al, 2006). Rubella virus is spread from person-to-person via the respiratory route and is the causative agent of rubella disease, commonly known as German measles (Lambert et al, 2015).…”
Section: Rubella Virus Classification Epidemiology Immunology and mentioning
confidence: 99%
“…Late immunity is shifted to predominantly proinflammatory cytokine profiles via increased concentrations of IL-6, granulocyte-macrophage colony-stimulating factor, and TNF-a, in combination with decreases in IL-10 (Dhiman et al, 2010). Human leukocyte antigens (HLAs), known to play critical roles in immune response to viruses, contribute to the heterogeneity of the immune response to rubella virus as a result of their polymorphic nature, whereby HLA class I and II polymorphisms restrict the available repertoire of rubella antigens presented to T cells and therefore influence the subsequent immune response (Mitchell et al, 1996;Ou et al, 1994Ou et al, , 1998. Current efforts are placed on deciphering the immunogenetics of antirubella humoral and cell-mediated immune responses, with a focus on better understanding HLA polymorphisms toward the development of vaccine candidates that utilize constructs comprised of HLA-specific epitopes that can induce immunity across heterogenetic populations, reviewed in Lambert et al (2015).…”
Section: Rubella Virus Classification Epidemiology Immunology and mentioning
confidence: 99%