Multiple alignment of the NS3 protein sequences in HCV strains.

(PDF)</p

Final selected CTL, HTL and LBL epitopes for multi-epitope vaccines construction.

Final selected CTL, HTL and LBL epitopes for multi-epitope vaccines construction.</p

S1 Fig -

Prediction of the secondary structure of the construct 1 (A) and construct 2 (B) vaccines. The predicted results showed that among 686 amino acids in the construct 1, 268 (39.07%), 135 (19.68%), 66 (9.62%) and 217 (31.63%) amino acids are involved in α-helix, extended strand, beta turn, and random coil, respectively. Our predicted outputs revealed that among 607 amino acids in the construct 2, 205 (33.77%), 132 (21.75%), 63 (10.38%) and 207 (34.10%) amino acids are involved in α-helix, extended strand, beta turn, and random coil, respectively. (DOCX)</p

Cytotoxic T Lymphocyte (CTL) epitopes of the P7protein.

(DOCX)</p

S2 Fig -

Linear (A and C) and Discontinuous (B and D) B-cell epitopes of the construct 1 (A and B) and construct 2 (C and D) vaccines (colored spheres). (DOCX)</p

Multiple alignment of the P7 protein sequences in HCV strains.

(PDF)</p

The 3D view of the final system conformations.

The interface residues between two proteins TLRs (orange cartoon) and vaccines (magenta cartoon) residues (orange and magenta sticks) are labeled. Hydrogen bonds and hydrophobic contacts are presented as green dashed line and arc with spokes radiating, respectively. A and B indicate TLR4-construct 1 and TLR3-construct 2 complexes, respectively.</p

Various features of multi-epitope vaccines.

Various features of multi-epitope vaccines.</p

Helper T Lymphocyte (HTL) epitopes of the NS3 protein.

(DOCX)</p

Multiple alignment of the NS5B protein sequences in HCV strains.

(PDF)</p