3iya

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Template:STRUCTURE 3iya

Contents 1 Association of the pr peptides with dengue virus blocks membrane fusion at acidic pH 2 Function 3 About this Structure 4 Reference

Association of the pr peptides with dengue virus blocks membrane fusion at acidic pH

Template:ABSTRACT PUBMED 19759134

Function

[POLG_DEN2U] 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).

About this Structure

3iya is a 6 chain structure with sequence from [1] and Aedes albopictus. Full crystallographic information is available from OCA.

Reference

• Yu IM, Holdaway HA, Chipman PR, Kuhn RJ, Rossmann MG, Chen J. Association of the pr peptides with dengue virus at acidic pH blocks membrane fusion. J Virol. 2009 Dec;83(23):12101-7. Epub 2009 Sep 16. PMID:19759134 doi:10.1128/JVI.01637-09