N-terminal GST fusion protein of PreM/M (Dengue virus 1)(a.a. 6-166)
DENV; DENV PreM/M Protein; DENV PreM/M; Dengue virus; Dengue virus PreM/M; DENV-1 PreM/M
> 95%, based on SDS PAGE
Before reconstitution, stable for 1 year at -20?C from the date of shipment. After reconstitution, stable for a month at 4?C.
The DENV prM (membrane) protein, which is important in the formation and maturation of the viral particle, consists of seven antiparallel β-strands stabilized by three disulphide bonds. The glycoprotein shell of the mature DENV virion consists of 180 copies each of the E protein and M protein. The immature virion starts out with the E and prM proteins forming 90 heterodimers that give a spiky exterior to the viral particle. This immature viral particle buds into the endoplasmic reticulum and eventually travels via the secretory pathway to the Golgi apparatus. As the virion passes through the trans-Golgi Network (TGN) it is exposed to low pH. This acidic environment causes a conformational change in the E protein which disassociates it from the prM protein and causes it to form E homodimers. These homodimers lie flat against the viral surface giving the maturing virion a smooth appearance. During this maturation pr peptide is cleaved from the M peptide by the host protease, furin. The M protein then acts as a transmembrane protein under the E-protein shell of the mature virion. The pr peptide stays associated with the E protein until the viral particle is released into the extracellular environment. This pr peptide acts like a cap, covering the hydrophobic fusion loop of the E protein until the viral particle has exited the cell.
DENV; DENV PreM/M Protein; DENV PreM/M; Dengue virus; Dengue virus PreM/M; DENV-1 PreM/M; DENV-1