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Envelope Protein (E)
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The E protein of avivirus is the major glycosylated structural protein (495 amino acid residues ($60 kDa for Den2) exposed on the surface of the virion. The E protein mediates receptor binding on the host cell surface, and at least for initial binding, cell-surface haparan sulfate proteoglycan seems important.47 Binding is followed by internalization of the virus via speci c receptor-mediated endocytosis, inducing fusion of the virion envelope with the host cell membrane, and virus entry. The E protein is a major target of the host cell response, containing hemagglutination and neutralizing antigenic epitopes conferring protective immunity, as well as non-neutralizing antigenic epitopes responsible for ADE.31,142 150 The E protein is therefore important for vaccine development as well as for diagnostic strategies. The E protein together with prM are on the surface of the virion, while the lipid bilayer and the viral capsid protein C tightly associated with viral RNA genome form the inner core of the virion.144,151 157 During virion morphogenesis, prM undergoes cleavage, mediated by furin-like protease, in a late trans-Golgi compartment, resulting in mature M protein, with a concomitant loss of the ectodomain of prM. The resultant mature particle is competent in fusion with the cell membrane.60,62,86,89,158 162 The presence of a avivirus receptor binding site on the envelope E was revealed by a clustering of mutations that affect virulence and analyses using monoclonal antibodies.38,42,143,150,163 165 The E protein of avivirus resembles the alphavirus E1 protein in possessing a class II viral fusion peptide. Structures of the dengue and TBE E proteins strongly suggest that aviviral E proteins are likely to have similar three-dimensional structures. The dengue E protein (Figure 10.6) is a dimer, arranged in three distinct domains, each of which forms a b barrel and is oriented parallel to the membrane. The central domain, I, consists of predominantly type-speci c non-neutralizing epitopes and is the molecular hinge region involved in low pH-induced conformational changes. The dimerization domain, II, makes contact with a copy of itself in the homodimer and is involved in virus-mediated membrane fusion. It contains many of the
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FIGURE 10.6 Structure of the E protein dimer. Beta strands in each monomer are represented by ribbons. Carbohydrate attached to the glycosylation site is not shown. (See insert for color representation.)
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cross-reactive epitopes recognized by neutralizing and non-neutralizing Mabs. Domain III has an immunoglobulin-like structure, containing the most distal projecting loops from the virion surface. This domain contains multiple typeand subtype-speci c epitopes, eliciting virus-neutralizing antibody response, and is thought to contain virus receptor binding site as well as being involved in tissue tropism. Several lines of evidence suggest that this overall structure of the E protein is conserved across Flaviviridae.144,148,151,152,166 After the virus binds to cellsurface receptors and is internalized into the endosome, the aviviral E homodimers are converted to a more stable homotrimeric form, as recently shown for both dengue and Semliki Forest viruses.149,167 The lower endosomal pH causes structural changes, which result in relative movements of domains I and III with respect to domain II (Figure 10.7) and bring the C terminus nearly 40 A closer to the fusion 149 The fusion loop inserts into the host cell loop, while exposing the loop. membrane, and the trimer is formed, initially through stabilizing interactions between the three fusion loops, propagating toward the base (Figure 10.8). This is followed by injection of viral RNA and replication.149 The structure of the Den virion also shows that the surface has an icosahedral symmetrical network of E homodimers.155
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FIGURE 10.7 Comparison of the structure of dengue 2 E protein monomer between preand postfusion conformations. (See insert for color representation.)
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