Norovirus Group-2

Norovirus Group-2 Capsid Recombinant
Cat. No.
BT29264
Source
Escherichia Coli.
Synonyms
Appearance
Sterile Filtered clear solution.
Purity

Protein is 95% pure as determined by 10% PAGE (coomassie staining).

Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

The Recombinant Norovirus Group-2 Capsid, E.Coli derived, is a positive sense RNA virus with 7.5kb nucleotides, encoding a major structural protein VP1 with 58~60kDa. The Recombinant Norovirus has two groups, group 1 and group 2. Group 2 recombinant capsid was derived from the full length capsid 53 to 548Aa.

Product Specs

Introduction
Human norovirus, categorized into group 1 and group 2, is a common cause of gastroenteritis. Norwalk virus, a group 1 species discovered in 1968, exemplifies this. Symptoms include vomiting, diarrhea, and nausea. The CDC estimates 19-21 million annual US infections, resulting in 800 deaths and a 1 in 15 infection rate. Globally, norovirus impacts roughly 267 million people, leading to over 200,000 deaths annually, primarily in developing countries and among vulnerable populations like children, the elderly, and immunocompromised individuals. Most cases resolve within days. Highly contagious, norovirus spreads through human contact, contaminated food/water, or surfaces. Outbreaks peak in January, typically occurring from November to April. This positive-sense RNA virus possesses 7.5kb nucleotides, encoding a major structural protein, VP1 (50-55kDa). VP1 comprises internal N-terminal, Hinge, shell (S), and protruding (P) domains. The P domain (225-520) forms a P1-P2-P1 structure and contains a receptor-binding region for human histo-blood group antigens (HBGAs). Bacterial expression of the P domain yields a P dimer and a P particle (12 P dimers), exhibiting higher HBGA binding affinity than virus-like particles (VLPs) from the full-length capsid. This makes the P domain promising for norovirus vaccine development.
Description
The Recombinant Norovirus Group-2 Capsid, derived from E. coli, is a positive-sense RNA virus with 7.5kb nucleotides. It encodes VP1, a major structural protein with a molecular weight of 58-60kDa. Noroviruses are classified into two groups. This recombinant capsid, from group 2, is derived from the full-length capsid, specifically amino acids 53 to 548.
Physical Appearance
Clear, sterile-filtered solution.
Formulation
PBS and 25mM K₂CO₃
Purity
The protein exhibits 95% purity as assessed by 10% SDS-PAGE with Coomassie blue staining.
Stability
For optimal storage, Recombinant Norovirus Group-2 should be kept at -18°C. While it remains stable at 4°C for up to one week, repeated freeze-thaw cycles should be avoided.
Source
Escherichia Coli.

Product Science Overview

Introduction

Noroviruses are a leading cause of acute nonbacterial gastroenteritis worldwide, affecting people of all ages. These viruses belong to the Caliciviridae family and are classified into several genogroups, with Genogroup II (GII) being one of the most prevalent and clinically significant. The capsid protein of noroviruses, particularly the major capsid protein VP1, plays a crucial role in the virus’s ability to infect host cells and elicit immune responses.

Structure and Function of Norovirus Capsid Proteins

The norovirus capsid is primarily composed of the VP1 protein, which forms virus-like particles (VLPs) when expressed recombinantly. The VP1 protein is divided into two main domains: the shell (S) domain and the protruding (P) domain. The S domain forms the structural core of the capsid, while the P domain extends outward and is involved in receptor binding and immune recognition .

Recombinant Expression of Norovirus Capsid Proteins

Recombinant expression systems have been developed to produce norovirus capsid proteins for research and vaccine development. These systems often use eukaryotic or prokaryotic hosts to express the VP1 protein, which then self-assembles into VLPs. These VLPs are morphologically and antigenically similar to native norovirus particles but lack the viral RNA, making them non-infectious .

Applications of Recombinant Norovirus Capsid Proteins
  1. Vaccine Development: Recombinant norovirus VLPs are being explored as potential vaccine candidates. They can elicit strong immune responses and have shown promise in preclinical and clinical trials.
  2. Diagnostic Tools: Recombinant capsid proteins are used in serological assays to detect norovirus-specific antibodies in human sera, aiding in the diagnosis of norovirus infections.
  3. Research: These proteins are invaluable in studying the interaction between noroviruses and host receptors, as well as in understanding the immune response to norovirus infections .
Challenges and Future Directions

Despite the progress made in the recombinant expression of norovirus capsid proteins, several challenges remain. One major challenge is the genetic diversity of noroviruses, which complicates the development of broadly protective vaccines. Additionally, the lack of a robust cell culture system for human noroviruses hinders the study of viral replication and pathogenesis .

Future research is focused on overcoming these challenges by developing more efficient expression systems, exploring novel adjuvants to enhance vaccine efficacy, and identifying conserved epitopes that can be targeted by broadly neutralizing antibodies .

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