Molecular basis of telaprevir resistance due to V36 and T54 mutations in the NS3-4A protease of the hepatitis C virus

Christoph Welsch^*¹^,2^,3 , Francisco S Domingues^*¹ , Simone Susser²^,3 , Iris Antes¹ , Christoph Hartmann¹ , Gabriele Mayr¹ , Andreas Schlicker¹ , Christoph Sarrazin²^,3 , Mario Albrecht¹ , Stefan Zeuzem²^,3 and Thomas Lengauer¹

¹Department of Computational Biology and Applied Algorithmics, Max Planck Institute for Informatics, 66123 Saarbrücken, Germany

²Department of Internal Medicine I, Johann Wolfgang Goethe University Hospital, 60590 Frankfurt/Main, Germany

³Department of Internal Medicine II, Saarland University Hospital, 66421 Homburg/Saar, Germany

author email corresponding author email* Contributed equally

Genome Biology 2008, 9:R16doi:10.1186/gb-2008-9-1-r16


Published:	23 January 2008

Subject areas: Biochemistry and structural biology, Bioinformatics, Medicine

Additional files

Additional data file 1:

Figure S1 illustrates NS3-4A protease-ligand interactions. Figure S2 shows the complete network of non-covalent, H-bond and van der Waals, interactions of the NS3-4A protease for the PDB entry 1RTL. Figure S3 gives results of SCH 503034 and VX-950 inhibitor studies using an HCV V36G mutant replicon assay. Table S1 lists HCV genotypes included into the multiple sequence alignment of Figure 9.

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