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  1. 26 kwi 2021 · This review focuses on the life cycle of RUBV with emphasis on recent findings on the structures of the virus particle and its component proteins and on the mechanisms of virus entry, fusion, assembly, and budding.

  2. Rubella virus contains three major structural polypeptides: two membrane glycoproteins, E1 and E2 and a single nonglycosylated RNA-associated capsid protein, C, within the virion. One of the envelope proteins, E1, is responsible for viral hemagglutination and neutralization.

  3. 26 kwi 2021 · Rubella virus (RUBV), a rubivirus, is an airborne human pathogen that generally causes mild measles-like symptoms in children or adults. However, RUBV infection of pregnant women can result in misc...

  4. 1 sty 2006 · Rubella virus (RV) is a member of the genus rubivirus in the family of togaviridae. It is a spherical particle of about 60-70nm in diameter. The particle is enveloped with a single-stranded polyadenylated genomic RNA of positive polarity composed of 9757 nucleotides in length, excluding the poly (A) tail and has a very high G/C content of 69.5%.

  5. 9 wrz 2010 · Viral factories are complex structures in the infected cell where viruses compartmentalize their life cycle. Rubella virus (RUBV) assembles factories by recruitment of rough endoplasmic reticulum (RER), mitochondria and Golgi around modified lysosomes known as cytopathic vacuoles or CPVs.

  6. 24 sty 2013 · Here we report the 1.8 Å resolution crystal structure of envelope glycoprotein E1, the main antigen and sole target of neutralizing antibodies against rubella virus. E1 is the main player during entry into target cells owing to its receptor-binding and membrane-fusion functions.

  7. Rubella virus contains three major structural polypeptides designated El, E2, and C with molecular weights of 62,000, 47,000-54,000 (a complex), and 38,000, respectively, as de-termined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reduced conditions. Limited-digest peptide maps confirm that each of these polypeptides is dis-

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