Anti-Murine Norovirus Capsid [Clone A6.2] - Purified <i>in vivo</i> PLATINUM™ Functional Grade (N272-GRP)

Norovirus, a Caliciviridae virus made up of a single major capsid protein (VP1), causes acute gastroenteritis during infection1. The capsid protein is composed of three structural domains: N (N terminus), S (shell), and P (protruding), with the latter further divided into P1 and P2 subdomains. P1 has moderate sequence diversity, while P2 is highly variable. Murine norovirus (MNV-1) is the first norovirus used to study the immune response in animal models and can infect the intestinal tract of mice following oral inoculation2. MNV-1 can infect macrophage-like cells in vivo and can be cultured in primary dendritic cells and macrophages. A6.2 was generated from an MNV-1-seropositive 129 mouse injected with brain homogenate containing MNV-12. The spleen was harvested, hybridoma fusion performed, and supernatants screened by ELISA for binding to recombinant MNV-1 capsid. A6.2 is a neutralizing antibody used for structural analysis of MNV in cryo-EM1,3,4,5,6 and NMR7 studies. Neutralization by A6.2 has also been demonstrated in plaque based assays2. A6.2 Fab can also neutralize MNV, albeit with 100 times lower efficacy than the intact antibody, showing that neutralization does not require bivalent binding. Additionally, neutralization of MNV with A6.2 Fab does not induce major conformational changes in the virion. Binding of glycochenodeoxycholic acid to MNV abrogates the neutralization capacity of A6.26,7. A6.2 is thought to neutralize MNV-1 infection by preventing virion attachment to the cell surface3. Phage-display oligopeptide library screens have been used to map the binding epitope to the P2 subdomain8. A6.2 does not react with capsid protein in Western blot analysis, and therefore likely binds to a 3D epitope1.