Alternative Name(s):

; Outer capsid protein VP4; Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]

Species: (Organism)

Rotavirus A (strain Human/United Kingdom/ST3/1975 G4-P2A[6]-I1-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A) (Rotavirus A (strain St. Thomas 3))

Gene Names:

N/A

Tag info:

N-terminal 6xHis-SUMO-tagged

Target Protein AA Sequence:

AQVSEDIIISKTSLWKEMQYNRDIIIRFKFNNSIIKLGGLGYKWSEISFKAANYQYNYLRDGEQVTAHTTCSVNGVNNFSYNGGLLPTHFSISRYEVIKENSYVYVDYWDDSQAFRNMVYVRSLAANLNSVKCSGGNYNFQMPVGAWPVMSGGAVSLHFAGVTLSTQFTDFVSLNSLRFRFSLTVEEPPFSILRTRVSGLYGLPASNPNSGHEYYEIAGRFSLISLVPSNDDY

Expression Region:

247-479aa

Subcellular Location:

Outer capsid protein VP4: Virion, Host rough endoplasmic reticulum, Note=Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7, these enveloped particles also contain VP4, As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple-layered particles (By similarity), SUBCELLULAR LOCATION: Outer capsid protein VP8*: Virion, Note=Outer capsid protein, SUBCELLULAR LOCATION: Outer capsid protein VP5*: Virion

Tissue Specificity:

Protein Length:

Partial

Pathway:

Mol. Weight:

42.3 kDa

Purity:

Greater than 90% as determined by SDS-PAGE.

Form:

Liquid or Lyophilized powder

Buffer:

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Research Areas:

Others

Function:

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 entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. According to the considered strain, VP4 seems to essentially target sialic acid and/or the integrin heterodimer ITGA2/ITGB1 (By similarity).

Involvement in disease:

Relevance:

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 entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. According to the considered strain, VP4 ses to essentially target sialic acid and/or the integrin heterodimer ITGA2/ITGB1 .Outer capsid protein VP5*: forms the spike "foot" and "body". Acts as a mbrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment .VP8* forms the head of the spikes. It is the viral hagglutinin and an important target of neutralizing antibodies. In sialic acid-dependent strains, VP8* binds to host cell sialic acid, most probably a ganglioside, providing the initial contact .

Reconstitution:

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Families:

Rotavirus VP4 family

Reference:

Sequence of the fourth gene of human rotaviruses recovered from asymptomatic or symptomatic infections.Gorziglia M., Green K.Y., Nishikawa K., Taniguchi K., Jones R.W., Kapikian A.Z., Chanock R.M.J. Virol. 62:2978-2984(1988)