The widespread rubella virus belongs to the family of Matonaviridae, formerly to Togaviridae. It is an enveloped, single-stranded RNA virus with three structural proteins: The capsid protein C interacts with genomic RNA and assembles into the icosahedral nucleocapsid, while the membrane-spanning glycoproteins E1 and E2 form the viral spike complexes. The E1-E2 heterodimers on the viral surface are the major targets for neutralizing antibodies during infection.
Rubella virus is transmitted by droplets. In populations with low vaccination uptake rates, the majority of infections occur in children. While severe complications in children are rare, Rubella virus infection during pregnancy can cause congenital rubella syndrome (CRS) with serious damage to fetuses. Consequently, the diagnosis of rubella infection during gestation is of considerable importance.
Specific IgM detection is essential for reliable rubella diagnostics. Unfortunately, many Rubella IgM assays show significant cross-reactivity towards other pathogens. It is believed that the capsid protein C is primarily responsible for these non-specific interferences in rubella assays.
Rubella Spike Ectodomain (E1-E2) antigen is a patented (DE 10 2019 004 812), capsid-free, highly pure recombinant antigen produced in insect cells. The sequence of the recombinant protein is derived from the rubella vaccine strain HPV-77 and combines the ectodomains of glycoproteins E1 and E2, which are the major immunological targets. The sequence and the eukaryotic expression system were carefully chosen to provide a reliable product for the development of highly specific IgG and IgM detection assays.
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