Product Name: Norovirus GI.1 VP1 Virus-Like Particles
Catalog Number: ACVL-VLP006
Category: Virus-Like Particles (VLPs)
Expression System: Baculovirus–Insect Cell Expression System
Purity: >90% (SDS-PAGE / HPLC)
Formulation: Supplied in Tris-based buffer
Product Overview
Norovirus GI.1 VP1 Virus-Like Particles (VLPs) are recombinant capsid assemblies produced by expressing the major structural protein VP1 in a baculovirus–insect cell system. The VP1 protein naturally self-assembles into highly ordered virus-like particles that closely resemble the morphology and antigenic surface of native norovirus virions.
These particles do not contain viral genomic RNA or non-structural proteins, making them completely non-infectious and replication-incompetent while preserving the authentic structural features of the viral capsid. As a result, Norovirus GI.1 VLPs provide a safe and reliable platform for studying viral antigenicity, capsid architecture, and immune recognition.
Each particle consists of approximately 180 VP1 monomers arranged into an icosahedral capsid, reproducing the external structure and epitope presentation of natural norovirus particles.
Structural Characteristics of VP1
VP1 is the principal capsid protein responsible for particle assembly and antigenic presentation. The protein contains several structural domains that coordinate capsid formation and host interactions.
Major structural regions include:
Forms the internal scaffold of the viral capsid and is essential for the formation of the icosahedral structure.
Extends outward from the capsid surface and mediates intermolecular contacts between VP1 dimers.
Contributes to capsid stability and structural integrity.
The most exposed and variable region of the capsid, often associated with host receptor binding and immune recognition.
The highly exposed P2 region is particularly important for studying antigenic variation, neutralizing antibody responses, and virus–host interactions.
Product Features
- Authentic virus-like particles that closely mimic native norovirus capsids
- Genome-free and non-infectious for safe laboratory handling
- High purity recombinant particles suitable for immunological applications
- Uniform VP1 self-assembly into stable VLP structures
- Consistent production using baculovirus–insect cell expression technology
Applications
Norovirus GI.1 VP1 VLPs are widely used in virology, immunology, and vaccine development research.
Typical applications include:
- Vaccine antigen development
- Immunogenicity evaluation in preclinical studies
- Serological assay development (ELISA and antibody detection)
- Neutralizing antibody screening
- Structural and antigenic characterization of capsid proteins
- Epitope mapping and receptor binding studies
Background
Noroviruses are small, non-enveloped, positive-sense RNA viruses belonging to the Caliciviridae family and represent one of the leading causes of acute viral gastroenteritis worldwide. Multiple genogroups and numerous genetic variants circulate globally, contributing to frequent outbreaks in community and healthcare settings.
Transmission typically occurs through contaminated food, water, surfaces, or direct person-to-person contact. Infection often results in rapid onset gastrointestinal symptoms including vomiting, diarrhea, nausea, and abdominal discomfort. Although symptoms generally resolve within several days, severe cases may occur in infants, elderly individuals, and immunocompromised patients.
The development of vaccines and antiviral therapies has been challenging due to the high genetic diversity of noroviruses and the limited availability of robust cell culture systems for viral propagation. As a result, virus-like particles (VLPs) have become essential research tools. By faithfully reproducing the structural properties of the viral capsid without containing infectious genetic material, VLPs enable detailed investigation of antigenicity, immune responses, and vaccine design.
GI.1 VLPs, together with other genotypes such as GII.4, are frequently used as experimental antigens in norovirus vaccine and immunology studies.
Our products and services are for research use only and cannot be used for any clinical purposes.
