Dengue virus receptors reported I different studies.

<p>Dengue virus receptors reported I different studies.</p

Structure-based alignment of the 400 non-redundant amino acid sequences of E proteins from Dengue Virus serotype 1–4.

<p>Dots indicate amino acid identities; dashes show gaps. The domains are indicated by a colored bar as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0059211#pone-0059211-g001" target="_blank">Fig. 1</a>. The conserved glycosylation site in domain II is indicated by a red asterisk and red lettering. Residues in box indicates epitopic region covering ASN 67. Residues that are conserved in All four serotypes of Dengue virus are colored in sky blue.</p

Dengue envelope glycoprotein and DC-SIGN interface.

<p>(<b>a</b>) Den-E-DC-SIGN Complex represented as a ribbon diagram are shown inCyan and Pink, respectively. (<b>b</b>) The Dengue envelope (chain A)-DC-SIGN binding interface. Side chains of the amino acids contributing to hydrogen bonding formation (indicated byblack dotted lines) are represented by a stick model with the residue names and numbers shown. (<b>c</b>) The Den-E (chain A)-DC-SIGN binding interface is also represented in a similar fashion as (<b>b</b>).</p

List of interfacing residues between Den-E-DC-SIGN-CRD complexes.

<p>Residues involved in the formation of H-bond are in bold while both bold and italic are involved in salt bridges.</p>*<p>Total change in surface area of the interface for a given chain. DSSP program <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0059211#pone.0059211-Kabsch1" target="_blank">[59]</a>.</p>**<p>Hydrophobicity index (mean). AAIndex database <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0059211#pone.0059211-Kawashima1" target="_blank">[60]</a>.</p

Maximum likelihood tree for the E gene from 123 flaviviruses

<p>. The tree is rooted by the sequence from <i>Aedes albopictus</i> cell fusion agent (CFA) virus.</p

ZDOCK confirmation results.

<p>Table enlists interfacing residues in both test (ZDOCK Docked) and PDB crystal structure of (pdb cod 3UZQ). Bold residues are involved in hydrogen bonding.</p

Dengue envelope glycoprotein and 2G12 antibody interface.

<p>(<b>a</b>) Den-E-2G12 Complex represented as a ribbon diagram are shown in Cyan and Pink and Green, respectively. (<b>b</b>) The Dengue envelope (chain A) and 2G12 light chain binding interface. Side chains of the amino acids contributing to hydrogen bonding formation (indicated by black dotted lines) are represented by a stick model with the residue names and numbers shown. (<b>c</b>) The Den-E and 2G12 heavy chain binding interface is also represented in a similar fashion as (<b>b</b>). (<b>d</b>)NAG sugar present at Den-E-2G12 interface.</p

Interaction and Inhibition of Dengue Envelope Glycoprotein with Mammalian Receptor DC-Sign, an In-Silico Approach

<div><p>Membrane fusion is the central molecular event during the entry of enveloped viruses into cells. The critical agents of this process are viral surface proteins, primed to facilitate cell bilayer fusion. The important role of Dendritic-cell-specific ICAM3-grabbing non-integrin (DC-SIGN) in Dengue virus transmission makes it an attractive target to interfere with Dengue virus Propagation. Receptor mediated endocytosis allows the entry of virions due to the presence of endosomal membranes and low pH-induced fusion of the virus. DC-SIGN is the best characterized molecule among the candidate protein receptors and is able to mediate infection with the four serotypes of dengue virus (DENV). Unrestrained pair wise docking was used for the interaction of dengue envelope protein with DC-SIGN and monoclonal antibody 2G12. Pre-processed the PDB coordinates of dengue envelope glycoprotein and other candidate proteins were prepared and energy minimized through AMBER99 force field distributed in MOE software. Protein-protein interaction server, ZDOCK was used to find molecular interaction among the candidate proteins. Based on these interactions it was found that antibody successfully blocks the glycosylation site ASN 67 and other conserved residues present at DC-SIGN-Den-E complex interface. In order to know for certain, the exact location of the antibody in the envelope protein, co-crystallize of the envelope protein with these compounds is needed so that their exact docking locations can be identified with respect to our results.</p> </div

Structure of the monomer of dengue E soluble fragment (sE) in the mature virus particle.

<p><b>A</b>, The three domains of dengue envelope, Domain I is magenta, domain II is yellow, domain III is red also indicated by bars above the figure. <b>B,</b> ASN 67-residue domain II links Dengue E to DC-SIGN Receptor on human dendritic cells. <b>C,</b> Structure of the carbohydrate recognition domain of human DC-SIGN attached by hydrogen bonds to mannose in green.</p

List of interfacing residues between Den-E-2G12 complexes.

<p>Residues involved in the formation of H-bond are in bold while both bold and italic are involved in salt bridges.</p>*<p>Total change in surface area of the interface for a given chain. DSSP program <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0059211#pone.0059211-Kabsch1" target="_blank">[59]</a>.</p>**<p>Hydrophobicity index (mean). AAIndex database <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0059211#pone.0059211-Kawashima1" target="_blank">[60]</a>.</p