First NGS full genome characterization of a hepatitis C virus genotype 7 divergent subtype.

We report the near full length genome sequence, of an hepatitis C virus isolate from a man originating from Democratic Republic of Congo, whose genotype could not be determined by the routinely used sequence technique.The near-complete genome sequence of this variant BAK1 was obtained by the association of two next generation sequencing technologies.Evolutionary analysis indicates that this isolate BAK1 could be the first reported strain belonging to a new HCV-7b subtype. This new subtype has been incorrectly identified as genotype 2 by Versant HCV Genotype 2.0 assay (LiPA).The requirement of three independent isolates has been filled and a new subtype can be assigned. More examples of HCV-7 are required to better understand its origin, its pathogenicity and its relationship with genotype 2

First NGS full genome characterization of a hepatitis C virus genotype 7 divergent subtype.

We report the near full length genome sequence, of an hepatitis C virus isolate from a man originating from Democratic Republic of Congo, whose genotype could not be determined by the routinely used sequence technique.The near-complete genome sequence of this variant BAK1 was obtained by the association of two next generation sequencing technologies.Evolutionary analysis indicates that this isolate BAK1 could be the first reported strain belonging to a new HCV-7b subtype. This new subtype has been incorrectly identified as genotype 2 by Versant HCV Genotype 2.0 assay (LiPA).The requirement of three independent isolates has been filled and a new subtype can be assigned. More examples of HCV-7 are required to better understand its origin, its pathogenicity and its relationship with genotype 2

First next-generation sequencing full-genome characterization of a hepatitis C virus genotype 7 divergent subtype

International audienc

Functional Interaction of Aurora-A and PP2A during Mitosis

Entry into mitosis is a highly regulated process, promoted by the activated Cyclin B1/Cdk1 complex. Activation of this complex is controlled, in part, by the protein kinase Aurora-A, which is a member of a multigenic serine/threonine kinase family. In normal cells, Aurora-A activity is regulated, at least in part, by degradation through the APC-ubiquitin-proteasome pathway. It has recently been proposed that, in Xenopus, Aurora-A degradation can be inhibited by phosphorylation. It would thus be expected that a phosphatase activity would release this blockade at the end of mitosis. Here, we have shown that the protein phosphatase PP2A and Aurora-A are colocalized at the cell poles during mitosis in human cells and interact within the same complex. Using the PP2A inhibitor okadaic acid and an RNAi approach, we have shown that this interaction is functional within the cell. PP2A/Aurora-A interaction is promoted by an S51D mutation in Aurora-A and inhibited by a phosphomimetic peptide centered around Aurora-A S51, thereby strongly suggesting that PP2A controls Aurora-A degradation by dephosphorylating serine 51 in the A box of the human enzyme