Structural highlights
Function
[Q66394_9FLAV] 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).[SAAS:SAAS011998_004_099774]
Publication Abstract from PubMed
Previous binding studies of antibodies that recognized partially or fully hidden epitope suggest that insect cells derived dengue virus undergoes structural changes at elevated temperature. This is confirmed by our cryo-electron microscopy images of dengue virus incubated at 37 degrees C, where viruses change their surface from smooth to rough. Here we present the cryo-electron microscopy structures of dengue virus at 37 degrees C. Image analysis showed four classes of particles. The 3D map of one of these classes, representing half of the imaged virus population, shows that the E protein shell has expanded and there is a hole at the 3-fold vertices. Fitting E protein structures into the map suggests that all the inter-dimeric and some intra-dimeric E protein interactions are weakened. The accessibility of some previously found cryptic epitopes on this class of particles is discussed.
Structural changes of dengue virus when exposed to 37{degrees}C.,Fibriansah G, Ng TS, Kostyuchenko VA, Lee J, Lee S, Wang J, Lok SM J Virol. 2013 May 1. PMID:23637405[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fibriansah G, Ng TS, Kostyuchenko VA, Lee J, Lee S, Wang J, Lok SM. Structural changes of dengue virus when exposed to 37{degrees}C. J Virol. 2013 May 1. PMID:23637405 doi:10.1128/JVI.00757-13
