Rate of patients with baseline RAVs for different DAA combination therapies.

<p>Rate of patients with baseline RAVs for different DAA combination therapies.</p

Occurrence of RAVs within <i>NS5A</i> in GT1a- (A) and GT1b- (B) infected patients.

<p>Occurrence of RAVs within <i>NS5A</i> in GT1a- (A) and GT1b- (B) infected patients.</p

Baseline <i>NS3</i> RAVs in DAA-naïve patients.

<p>A) GT1a- and B) GT1b-infected patients.</p

Patient characteristics at baseline.

<p>Patient characteristics at baseline.</p

Prevalence of <i>NS5B</i> RAVs in GT1a- (A) and GT1b- (B) infected patients.

<p>Prevalence of <i>NS5B</i> RAVs in GT1a- (A) and GT1b- (B) infected patients.</p

Association of <i>HLA-DPA1</i> variant rs3077 and <i>HLA-DPB1</i> variant rs9277535 with HBV infection.

*<p>controls include either healthy subjects with negative serological HBV markers (vs. HBV patients) or inactive HBsAg carriers in the subgroup analysis of patients with HBV infection (vs. active CHB patients);</p>**<p>to sustain the conventional gene description from the 5′ end to the 3′ end we changed the SNP denomination in comparison to previous publications. That is, the rs3077T/C alleles in our study correspond to the A/G alleles, respectively, in previously published studies <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0032605#pone.0032605-Kamatani1" target="_blank">[9]</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0032605#pone.0032605-Guo1" target="_blank">[11]</a>.</p

Clinical characteristics of patients with persistent HBV infection (n = 201).

<p>Characteristics are shown for all patients as well as inactive HBsAg carriers (n = 48) and active CHB patients (n = 46) in whom longitudinal data were available.</p><p>IC, inactive HBsAg carriers; CHB, active chronic hepatitis B;</p>*<p>HBV genotype was available in 67 patients (25 in IC and 18 in CHB).</p

Rotameric states and conformational differences for V36 mutants A/G/L/M computed with IRECS using the PDB entry

The figure illustrates the relative position of mutant side chains (light grey) and the wild-type residue V36 (blue). The important carbon atoms of the side chains are indicated as C, Cand C. Protein backbone changes are depicted in black. The contribution of F43 to the hydrophobic cavity conformation and the cyclopropyl binding pocket is illustrated by means of a transparent surface patch.<p><b>Copyright information:</b></p><p>Taken from "Molecular basis of telaprevir resistance due to V36 and T54 mutations in the NS3-4A protease of the hepatitis C virus"</p><p>http://genomebiology.com/2008/9/1/R16</p><p>Genome Biology 2008;9(1):R16-R16.</p><p>Published online 23 Jan 2008</p><p>PMCID:PMC2395260.</p><p></p

NS3-4A protease domain of PDB structure with co-crystallized ligand CPX (yellow) 32 and a second ligand, SCH 446211 (light blue), taken from the superimposed PDB structure 30

The protease binding pocket from structure is shown as a transparent surface patch. The residues V36 and T54 are depicted as stick-and-ball models, located in the parallel β-strands β1 and β3 of an anti-parallel β-sheet (dark blue).<p><b>Copyright information:</b></p><p>Taken from "Molecular basis of telaprevir resistance due to V36 and T54 mutations in the NS3-4A protease of the hepatitis C virus"</p><p>http://genomebiology.com/2008/9/1/R16</p><p>Genome Biology 2008;9(1):R16-R16.</p><p>Published online 23 Jan 2008</p><p>PMCID:PMC2395260.</p><p></p

Network of non-covalent residue interactions for the NS3-4A protease and the corresponding list of protein-ligand interactions

Network analysis of non-covalent residue interactions for the NS3-4A protease (PDB entry ). Nodes represent residues and colored edges represent different types of interactions: van der Waals interactions, backbone-side chain (blue), side chain-side chain (red); H-bond interactions, backbone-side chain (green), side chain-side chain (orange). Protein-ligand interactions for the and ligands CPX and SCH 446211, respectively, as well as for VX-950 are tagged by brown Arabic numerals above each residue node (see (b)). Catalytic residues are yellow and the mutated residues are blue (V36), red (T54) and grey (R155, A156). List of van der Waals interactions (vdW), H-bonds (HB) and covalent bonds (CB) for the and ligands CPX and SCH 446211, respectively, and the VX-950 ligand docking result. Each dot or square represents one interaction of the ligand with an amino acid of the NS3-4A protease, and dots indicate interactions with the cyclopropyl group. Brown Arabic numerals refer to protein-ligand interactions in the network of non-covalent interactions (a).<p><b>Copyright information:</b></p><p>Taken from "Molecular basis of telaprevir resistance due to V36 and T54 mutations in the NS3-4A protease of the hepatitis C virus"</p><p>http://genomebiology.com/2008/9/1/R16</p><p>Genome Biology 2008;9(1):R16-R16.</p><p>Published online 23 Jan 2008</p><p>PMCID:PMC2395260.</p><p></p