Genome Polyprotein (NS1) Dengue Virus Type 2 Recombinant Protein

Function: Capsid protein C packages viral RNA to form a viral nucleocapsid, and promotes virion budding

By similarity.prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated

By similarity.Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes

By similarity.Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Soluble and membrane-associated NS1 may activate human complement and induce host vascular leakage. This effect might explain the clinical manifestations of dengue hemorrhagic fever and dengue shock syndrome

By similarity.

Subunit structure: Capsid protein C forms homodimers. prM and envelope protein E form heterodimers in the endoplasmic reticulum and Golgi. In immature particles, there are 60 icosaedrally organized trimeric spikes on the surface. Each spike consists of three heterodimers of envelope protein M precursor (prM) and envelope protein E. NS1 forms homodimers as well as homohexamers when secreted

By similarity.

Subcellular location: Capsid protein C: Virion

Potential. Peptide pr: Secreted

By similarity. Small envelope protein M: Virion membrane; Multi-pass membrane protein

By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein

By similarity. Envelope protein E: Virion membrane; Multi-pass membrane protein

By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein

By similarity. Non-structural protein 1: Secreted. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side

By similarity.

Domain: Transmembrane domains of the small envelope protein M and envelope protein E contains an endoplasmic reticulum retention signals

By similarity.

Post-translational modification: Specific enzymatic cleavages in vivo yield mature proteins. The nascent protein C contains a C-terminal hydrophobic domain that act as a signal sequence for translocation of prM into the lumen of the ER. Mature protein C is cleaved at a site upstream of this hydrophobic domain by NS3. prM is cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr

By similarity.Envelope protein E and non-structural protein 1 are N-glycosylated

By similarity.