Norovirus Group-1 P-Domain
Description
The Recombinant Norovirus Group-1 Capsid P-Domain, E.Coli derived, Norwalk strain contains a.a. from 225-520 having a Mw of 30kDa. The protein is fused to a 6xHis tag at N-terminal and purified by chromatography techniques.
P-domain (225-520 a.a.) forms P1- P2-P1 structure. P-domain has a receptor binding region to recognize human histo-blood group antigens (HBGAs). P-domain expressed in
bacteria can spontaneously form a P dime and a P particle aggregated by 12 P dimmers. P-particle displays an enhanced binding activity to HBGAs higher than virus-like particle
(VLP) formed by the full length capsid.
Product Specs
Human norovirus is a common cause of gastroenteritis, leading to symptoms like vomiting and diarrhea. Classified into two groups (1 and 2), its discovery dates back to 1968 in Ohio with the identification of the Norwalk virus, a group 1 member. This virus significantly impacts global health, infecting millions and causing a considerable number of deaths annually, particularly in vulnerable populations. Transmission occurs through contaminated food, water, or surfaces, with peak infection rates during specific seasons. Norovirus, a positive-sense RNA virus, possesses a protein called VP1 crucial for its structure. This protein contains a region known as the P domain, which plays a vital role in binding to human cells. Notably, the P domain can independently assemble into particles, showing promise for vaccine development.
This recombinant Norovirus Group-1 Capsid P-Domain protein, derived from E. coli, represents the Norwalk strain and spans amino acids 225 to 520, resulting in a molecular weight of 30kDa. A 6xHis tag is attached to the protein's N-terminal for purification purposes. This P-domain exhibits a specific structure and contains a region responsible for binding to human cell receptors. Interestingly, when expressed in bacteria, this domain can self-assemble into larger particles, exhibiting enhanced binding capabilities compared to particles formed from the full-length capsid protein.
The protein is supplied in a buffer containing phosphate and 10 mM K2CO3.
While the recombinant Norovirus Group-1 P-Domain remains stable at 4°C for up to one week, storage at -18°C or below is recommended. Repeated freezing and thawing should be avoided to preserve protein integrity.
Product Science Overview
Norovirus is a highly contagious virus that causes gastroenteritis, an inflammation of the stomach and intestines leading to symptoms such as vomiting, diarrhea, and stomach pain. It is a positive-sense RNA virus with a genome size of approximately 7.5 kilobases. Norovirus is classified into ten genogroups (GI-GX), with genogroups I, II, IV, VIII, and IX infecting humans .
The P-domain of the norovirus capsid is crucial for the virus’s ability to bind to human histo-blood group antigens (HBGAs), which are receptors on the surface of human cells. This binding is essential for the virus to infect host cells. The P-domain can be expressed in bacteria and can spontaneously form P dimers and P particles, which display enhanced binding activity to HBGAs compared to virus-like particles (VLPs) formed by the full-length capsid .
The recombinant Norovirus Group-1 Capsid P-Domain is derived from the Norwalk strain and is expressed in Escherichia coli. It contains amino acids from positions 225 to 520 of the VP1 protein, forming the P1-P2-P1 structure. The recombinant protein is fused to a 6xHis tag at the N-terminal and purified using chromatography techniques .
The recombinant P-domain is a valuable tool in norovirus research and vaccine development. Its ability to form P particles with enhanced binding activity to HBGAs makes it a promising candidate for vaccine development. Researchers can use the recombinant P-domain to study the virus’s binding mechanisms and to develop vaccines that elicit an immune response against the virus .
