Recombinant Rotavirus X VP4 protein (His tag) is a Human rotavirus B219 Fragment protein, in the 1 to 249 aa range, expressed in Yeast, with >85% purity and suitable for SDS-PAGE.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Outer capsid protein VP4. Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. It is subsequently lost, together with VP7, following virus entry into the host cell. Following entry into the host cell, low intracellular or intravesicular Ca(2+) concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7. Outer capsid protein VP5*. Forms the spike 'foot' and 'body' and acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. During entry, the part of VP5* that protrudes from the virus folds back on itself and reorganizes from a local dimer to a trimer. This reorganization may be linked to membrane penetration. Outer capsid protein VP8*. Forms the head of the spikes and mediates the recognition of specific host cell surface glycans. It is the viral hemagglutinin and an important target of neutralizing antibodies.
Outer capsid protein VP4, Hemagglutinin
Recombinant Rotavirus X VP4 protein (His tag) is a Human rotavirus B219 Fragment protein, in the 1 to 249 aa range, expressed in Yeast, with >85% purity and suitable for SDS-PAGE.
pH: 7.2 - 7.4
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
Outer capsid protein VP4
Belongs to the rotavirus VP4 family.
Outer capsid protein VP4
Rotavirus VP4 also known as rotaviral attachment protein is a structural protein of the rotavirus. It plays an important role in the virus's ability to infect host cells. This protein has an approximate molecular mass of 88 kDa. VP4 expresses on the outer surface of the rotavirus where it functions as a spike protein mediating attachment to cells and facilitating viral entry through membrane penetration. Its structural characteristics allow it to undergo conformational changes necessary for these processes.
The infectivity of rotaviruses depends significantly on the activity of VP4. VP4 forms part of a complex with the viral capsid proteins including VP6 and VP7 contributing to the stability and infection potential of the virus. The protein is cleaved by trypsin into two subunits VP5* and VP8* which increases the virus's ability to bind and penetrate host cells. This cleavage is an important step in the viral life cycle enhancing the infectivity of the virus.
The mechanism of VP4 is tightly linked to cellular pathways involving viral entry and replication. During infection VP4's interaction with cell surface molecules facilitates the entry of the virus directly impacting viral proliferation pathways. It shows significant interaction with cellular receptors like integrins which play a role in cell adhesion processes and signal transduction. These interactions can influence downstream effects on host cell functions and viral replication efficiency.
VP4 is a central factor in rotavirus-associated gastroenteritis a leading cause of severe diarrhea in infants and young children. The protein's ability to mediate viral entry into gastrointestinal epithelial cells makes it a target for vaccine development aimed at preventing rotavirus infections. The protein also interacts closely with NSP4 another rotavirus protein that acts as an enterotoxin exacerbating the symptoms of infection. Understanding the role of VP4 can provide insights into designing therapies to mitigate the impact of rotavirus-induced diseases.
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(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel of ab238376.
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