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Language
- English (12)
Has Fulltext
- yes (12)
Is part of the Bibliography
- no (12)
Keywords
- ACLF (1)
- Electron-pion identification (1)
- Fibre/foam sandwich radiator (1)
- Ionisation energy loss (1)
- Multi-wire proportional drift chamber (1)
- NASH (1)
- Neural network (1)
- Single-molecule biophysics (1)
- Super-resolution microscopy (1)
- TR (1)
Institute
Schierwagen, Robert ; Uschner, Frank Erhard ; Ortiz, Cristina ; Torres Núñez, Sandra ; Brol, Maximilian ; Tyc, Olaf ; Gu, Wenyi ; Grimm, Christian ; Zeuzem, Stefan ; Plamper, Andreas ; Pfeifer, Philipp ; Zimmer, Sebastian ; Welsch, Christoph ; Schäfer, Liliana ; Rheinwalt, Karl P. ; Clària, Joan ; Arroyo, Vicente ; Trebicka, Jonel ; Klein, Sabine
The macrophage-inducible C-type lectin (mincle) is part of the innate immune system and acts as a pattern recognition receptor for pathogen-associated molecular patterns (PAMPS) and damage-associated molecular patterns (DAMPs). Ligand binding induces mincle activation which consequently interacts with the signaling adapter Fc receptor, SYK, and NF-kappa-B. There is also evidence that mincle expressed on macrophages promotes intestinal barrier integrity. However, little is known about the role of mincle in hepatic fibrosis, especially in more advanced disease stages. Mincle expression was measured in human liver samples from cirrhotic patients and donors collected at liver transplantation and in patients undergoing bariatric surgery. Human results were confirmed in rodent models of cirrhosis and acute-on-chronic liver failure (ACLF). In these models, the role of mincle was investigated in liver samples as well as in peripheral blood monocytes (PBMC), tissues from the kidney, spleen, small intestine, and heart. Additionally, mincle activation was stimulated in experimental non-alcoholic steatohepatitis (NASH) by treatment with mincle agonist trehalose-6,6-dibehenate (TDB). In human NASH, mincle is upregulated with increased collagen production. In ApoE deficient mice fed high-fat western diet (NASH model), mincle activation significantly increases hepatic collagen production. In human cirrhosis, mincle expression is also significantly upregulated. Furthermore, mincle expression is associated with the stage of chronic liver disease. This could be confirmed in rat models of cirrhosis and ACLF. ACLF was induced by LPS injection in cirrhotic rats. While mincle expression and downstream signaling via FC receptor gamma, SYK, and NF-kappa-B are upregulated in the liver, they are downregulated in PBMCs of these rats. Although mincle expressed on macrophages might be beneficial for intestinal barrier integrity, it seems to contribute to inflammation and fibrosis once the intestinal barrier becomes leaky in advanced stages of chronic liver disease.
Dultz, Georg ; Shimakami, Tetsuro ; Schneider, Markus ; Murai, Kazuhisa ; Yamane, Daisuke ; Marion, Antoine ; Zeitler, Tobias M. ; Stross, Claudia ; Grimm, Christian ; Richter, Rebecca M. ; Bäumer, Katrin ; Yi, MinKyung ; Biondi, Ricardo M. ; Zeuzem, Stefan ; Tampé, Robert ; Antes, Iris ; Lange, Christian ; Welsch, Christoph
Inhibitors against the NS3-4A protease of hepatitis C virus (HCV) have proven to be useful drugs in the treatment of HCV infection. Although variants have been identified with mutations that confer resistance to these inhibitors, the mutations do not restore replicative fitness and no secondary mutations that rescue fitness have been found. To gain insight into the molecular mechanisms underlying the lack of fitness compensation, we screened known resistance mutations in infectious HCV cell culture with different genomic backgrounds. We observed that the Q41R mutation of NS3-4A efficiently rescues the replicative fitness in cell culture for virus variants containing mutations at NS3-Asp168. To understand how the Q41R mutation rescues activity, we performed protease activity assays complemented by molecular dynamics simulations, which showed that protease-peptide interactions far outside the targeted peptide cleavage sites mediate substrate recognition by NS3-4A and support protease cleavage kinetics. These interactions shed new light on the mechanisms by which NS3-4A cleaves its substrates, viral polyproteins and a prime cellular antiviral adaptor protein, the mitochondrial antiviral signaling protein MAVS. Peptide binding is mediated by an extended hydrogen-bond network in NS3-4A that was effectively optimized for protease-MAVS binding in Asp168 variants with rescued replicative fitness from NS3-Q41R. In the protease harboring NS3-Q41R, the N-terminal cleavage products of MAVS retained high affinity to the active site, rendering the protease susceptible for potential product inhibition. Our findings reveal delicately balanced protease-peptide interactions in viral replication and immune escape that likely restrict the protease adaptive capability and narrow the virus evolutionary space.