Norovirus is a member of the Caliciviridae family and is responsible for gastroenteritis outbreaks. Murine norovirus (MNV-1) that is about 28 to 35 nm in diameter, shares many biochemical and genetic features with human noroviruses. An analysis of the MNV-1 genome shows three open reading frames (ORF) that are characteristic of noroviruses and vesiviruses. ORF1 is reported to encode a predicted 187 kDa polyprotein that contains the 2C helicase, 3C protease, and 3D polymerase motifs. ORF2 encodes a 59 kDa capsid protein that can self-assemble into virus-like particles when expressed in a baculovirus expression system. ORF3 is reported to encode a putative 22 kDa basic protein. The norovirus capsid protein contains a highly conserved shell (S) and protruding (P) domain and the P domain is shown to contain binding sites for receptors and neutralizing antibodies. The S domain is shown to be highly conserved and the capsid sequence diversity is limited to the P domain. MNV-1 infection is reported to modulate the MAPK pathway to activate eIF4E phosphorylation and the activation of p38 and Mnk during MNV-1 infection is considered to be important for its replication. This monoclonal antibody, clone 4F9.4, recognizes the P domain portion of the viral capsid protein and effectively neutralize MNV-1 and WU20 strains. It can also neutralize recombinant viruses V339I and D348E at higher doses. (Ref.: Kolawole, AO et al. (2014). J. Gen. Virol. 95(9); 1958-1968).，官网链接：https://www.sigmaaldrich.cn/product/mm/mabf2096 默克 科研、开发、生产。 作为生命科学行业的全球领先供应商，我们致力于为科研、生物技术开发和生产，以及制药药物疗法开发和生产提供各类解决方案和服务。

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