PMID:23300717

Citation	Tsai, WY, Hsieh, SC, Lai, CY, Lin, HE, Nerurkar, VR and Wang, WK (2012) C-Terminal Helical Domains of Dengue Virus Type 4 E Protein Affect the Expression/Stability of prM Protein and Conformation of prM and E Proteins. PLoS ONE 7:e52600
Abstract	The envelope (E) protein of dengue virus (DENV) is the major immunogen for dengue vaccine development. At the C-terminus are two α-helices (EH1 and EH2) and two transmembrane domains (ET1 and ET2). After synthesis, E protein forms a heterodimer with the precursor membrane (prM) protein, which has been shown as a chaperone for E protein and could prevent premature fusion of E protein during maturation. Recent reports of enhancement of DENV infectivity by anti-prM monoclonal antibodies (mAbs) suggest the presence of prM protein in dengue vaccine is potentially harmful. A better understanding of prM-E interaction and its effect on recognition of E and prM proteins by different antibodies would provide important information for future design of safe and effective subunit dengue vaccines.
Links	PubMed PMC3530441 Online version:10.1371/journal.pone.0052600
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
9FLAV:A0MNX0		GO:0036338: viral membrane	ECO:0000314:		C		Figure 1: Confirms the relationship between Protein E and prM. Protein E's function is an envelope protein and helps in protecting.This is also proven in Figure E.	complete CACAO 6501
DEN4T:POLG		GO:0030683: evasion or tolerance by virus of host immune response	ECO:0000315:		P		Fig 6 & 7	complete CACAO 6694
DEN4T:POLG	involved_in	GO:0030683: evasion or tolerance by virus of host immune response	ECO:0000315: mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete

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