10.1371/journal.ppat.1003359.g010
Simon Reiss
Simon
Reiss
Christian Harak
Christian
Harak
Inés Romero-Brey
Inés
Romero-Brey
Danijela Radujkovic
Danijela
Radujkovic
Rahel Klein
Rahel
Klein
Alessia Ruggieri
Alessia
Ruggieri
Ilka Rebhan
Ilka
Rebhan
Ralf Bartenschlager
Ralf
Bartenschlager
Volker Lohmann
Volker
Lohmann
Model of the interplay between NS5A and PI4KIIIα.
Public Library of Science
2013
Biochemistry
enzymes
Enzyme regulation
lipids
Lipid metabolism
metabolism
proteins
microbiology
Virology
Viral replication
Viral replication complex
Virulence factors and mechanisms
Molecular cell biology
Membranes and sorting
Infectious diseases
Viral diseases
hepatitis
Hepatitis C
interplay
ns5a
2013-05-09 00:15:35
Figure
https://plos.figshare.com/articles/figure/_Model_of_the_interplay_between_NS5A_and_PI4KIII_945_/700935
<p>A: Consensus sequence (red) of the PI4KIIIα interaction site (PFIS) derived from 672 NS5A sequences of all genotypes in the Los Alamos HCV database (<a href="http://hcv.lanl.gov" target="_blank">http://hcv.lanl.gov</a>). Green numbers in the top line refer to the degree of conservation (rounded). Numbers on the left and right refer to the positions of the flanking amino acids within NS5A. Variations from the consensus are listed according to their frequency. A proline found in the JFH-1 PFIS is marked in blue. Variants found only once are not shown. B: NS5A (light brown) interacts with PI4KIIIα (red). This interaction regulates NS5A phosphorylation status directly or indirectly. Active kinase promotes NS5A p56 formation, a fraction of which is hyperphosphorylated resulting in p58. P56 might positively influence viral RNA replication either directly or by affecting the morphology of the replication sites, for which additional host factors are probably required. PI4KIIIα interaction with NS5A and NS5B is required to trigger lipid kinase activity. This leads to formation of new PI4P pools, presumably involved in membranous web morphology.</p>