Anti-Norovirus Capsid蛋白VP1抗体[NVGC-01] (ab272687)

Norovirus is an RNA virus of the Caliciviridae taxonomic family, causes approximately 90% of epidemic non bacterial outbreaks of gastroenteritis around the world and is responsible for 50% of all foodborne outbreaks of gastroenteritis in the US. Norovirus affects people of all ages. The viruses are transmitted by faecally contaminated food or water and by person to person contact. Noroviruses contain a positive-sense RNA genome of approximately 7.5 kbp, encoding a major structural protein (VP1) of about 58~60 kDa and a minor capsid protein (VP2). The virus particles demonstrate an amorphous surface structure when visualized using electron microscopy and are between 27-38 nm in size. Capsid protein VP1 attaches virion to target cells by binding histo-blood group antigens present on gastroduodenal epithelial cells. Soluble capsid protein may play a role in viral immunoevasion. Capsid protein VP1 binds to histoblood group antigens at surface of target cells. The shell domain (S domain) contains elements essential for the formation of the icosahedron. The Protruding domain (P domain) is divided into subdomains P1 and P2. P domain interacts in dimeric contacts that increase the stability of the capsid and form the protrusions on the virion. An hypervariable region in P2 is thought to play an important role in receptor binding and immune reactivity.