Norovirus Group-2 P-Domain
Description
The Recombinant Norovirus Group-2 Capsid P-Domain, E.Coli derived, VA387 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, categorized into two groups. Norwalk virus, discovered in 1968, belongs to group 1. This virus leads to symptoms like vomiting, diarrhea, and nausea. The CDC estimates 19-21 million annual norovirus infections in the US, resulting in 800 deaths. Globally, it impacts around 267 million people, causing over 200,000 deaths, primarily in developing nations and vulnerable populations. Most cases resolve within a few days. Norovirus is highly contagious, spreading through contaminated food, water, or surfaces. Outbreaks peak in January, occurring mainly between November and April. This positive-sense RNA virus has a 7.5 kb genome encoding a major structural protein, VP1 (50-55kDa). VP1's structure comprises the N-terminal, Hinge, shell (S), and protruding (P) domains. The P domain (amino acids 225-520) forms a P1-P2-P1 structure and contains a receptor-binding region for human histo-blood group antigens (HBGAs). When expressed in bacteria, the P domain can form a P dimer and a P particle (12 P dimers). The P particle exhibits higher HBGA binding affinity than the virus-like particle (VLP) formed by the full-length capsid, making it a promising candidate for norovirus vaccine development.
This recombinant Norovirus Group-2 Capsid P-Domain, derived from E. coli strain VA387, consists of amino acids 225-520 and has a molecular weight of 30kDa. A 6xHis tag is fused to the N-terminal for purification using chromatography. The P-domain (225-520 a.a.) forms a P1-P2-P1 structure and possesses a receptor-binding region for recognizing human histo-blood group antigens (HBGAs). When expressed in bacteria, the P-domain can spontaneously form a P dimer and a P particle composed of 12 P dimers. This P-particle exhibits an enhanced binding affinity for HBGAs compared to the virus-like particle (VLP) formed by the full-length capsid.
The solution is formulated with a phosphate buffer and 17mM potassium carbonate (K2CO3).
For short-term storage, the Recombinant Norovirus Group-2 P-Domain remains stable at 4°C for up to one week. However, for long-term storage, it is recommended to store the protein below -18°C. Repeated freezing and thawing of the protein should be avoided.
Product Science Overview
Noroviruses (NoVs) are a group of single-stranded, positive-sense RNA viruses belonging to the Caliciviridae family. They are the leading cause of viral acute gastroenteritis worldwide, affecting millions of people annually. Noroviruses are divided into two major genogroups, GI and GII, with GII.4 being the predominant genotype responsible for the majority of outbreaks .
The norovirus capsid is primarily composed of a major structural protein known as VP1, which is approximately 60 kDa in size. This protein is responsible for forming the viral capsid and is encoded by the viral genome. The capsid protein is divided into two main domains: the shell (S) domain and the protruding (P) domain .
The P-domain is further subdivided into two subdomains, P1 and P2. The P2 subdomain is particularly important as it contains the most variable sequences and is located on the surface of the capsid. This subdomain plays a crucial role in immune recognition and receptor interaction .
The P-domain forms dimers and binds to histo-blood group antigens (HBGAs), which are recognized as receptors or attachment factors for noroviruses. This interaction is essential for the virus’s ability to infect host cells .
Studies have shown that the P-domain dimers exhibit broad specificity for HBGAs and bind to various oligosaccharides with different affinities. This binding is influenced by the type and structure of the HBGAs . The high yield and easy production of recombinant P-domain proteins make them ideal for research purposes.
Further research on the P-domain can provide valuable insights into the mechanisms of norovirus infection and aid in the development of effective vaccines and antiviral treatments .
