## Abstract The morphogenetic pathway of hepatitis A virus (HAV), classified as a member of the enteroviruses within the __Picornaviridae__, still remains obscure and seems to differ considerably from that of poliovirus, the most studied representative of this genus. In order to elucidate the precu
Recombinant proteins VP1 and VP3 of hepatitis A virus prime for neutralizing response
✍ Scribed by Dr. Verena Gauss-Müller; Zhou Mingquan; Klaus von der Helm; Friedrich Deinhardt
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 627 KB
- Volume
- 31
- Category
- Article
- ISSN
- 0146-6615
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
Six overlapping genomic regions of capsid proteins VP1 and VP3 of hepatitis A virus (HAV) inserted into the expression vectors pBD or pUR respectively expressed β‐galactosidase‐HAV fusion proteins. The recombinant proteins were poorly soluble so they were difficult to detect by human anti‐HAV sera in radioimmunoassay, but the fusion proteins dissolved in sodium dodecyl sulfate reacted with human and rabbit anti‐HAV‐positive sera in immunoblots. Antisera against VP1 and VP3 recombinant proteins reacted with the respective structural proteins of HAV in immunoblots. Two recombinant proteins, one including the first 120 amino acids of the N‐terminus of VP1 and the other containing all of VP1 except for the first 60 N‐terminal amino acids, induced a transient neutralizing antibody response in rabbits. Antisera directed against other regions of VP1 and VP3 neither neutralized viral infectivity nor recognized native virus in a competitive radioimmunoassay. However, when immunized animals were challenged with a subimmunogenic dose of HAV, all animals responded with stable virus‐neutralizing antibodies.
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