scholarly journals Effect of hepatitis E virus infection on the human hepatic innate immune response in human liver chimeric mice

2017 ◽  
Vol 66 (1) ◽  
pp. S246
Author(s):  
I.M. Sayed ◽  
L. Verhoye ◽  
L. Cocquerel ◽  
F. Abravanel ◽  
L. Foquet ◽  
...  
2015 ◽  
Vol 62 ◽  
pp. S522-S523
Author(s):  
L. Allweiss ◽  
S. Gass ◽  
T. Volz ◽  
K. Giersch ◽  
J. Kah ◽  
...  

2015 ◽  
Vol 53 (01) ◽  
Author(s):  
S Gass ◽  
T Volz ◽  
K Giersch ◽  
L Allweiss ◽  
A Lohse ◽  
...  

2016 ◽  
Vol 64 (5) ◽  
pp. 1033-1040 ◽  
Author(s):  
Lena Allweiss ◽  
Sofia Gass ◽  
Katja Giersch ◽  
Anne Groth ◽  
Janine Kah ◽  
...  

2021 ◽  
Vol 22 (17) ◽  
pp. 9259
Author(s):  
Pradip Devhare ◽  
Mridula Madiyal ◽  
Chiranjay Mukhopadhyay ◽  
Shiran Shetty ◽  
Shamee Shastry

Hepatitis E virus (HEV) usually causes self-limiting acute hepatitis, but the disease can become chronic in immunocompromised individuals. HEV infection in pregnant women is reported to cause up to 30% mortality, especially in the third trimester. Additionally, extrahepatic manifestations like neuronal and renal diseases and pancreatitis are also reported during the course of HEV infection. The mechanism of HEV pathogenesis remains poorly understood. Innate immunity is the first line of defense triggered within minutes to hours after the first pathogenic insult. Growing evidence based on reverse genetics systems, in vitro cell culture models, and representative studies in animal models including non-human primates, has implicated the role of the host’s innate immune response during HEV infection. HEV persists in presence of interferons (IFNs) plausibly by evading cellular antiviral defense. This review summarizes our current understanding of recognizing HEV-associated molecular patterns by host cell Pattern Recognition Receptors (PRRs) in eliciting innate immune response during HEV infection as well as mechanisms of virus-mediated immune evasion.


2017 ◽  
Vol 91 (21) ◽  
Author(s):  
Promisree Choudhury ◽  
Luke D. Bussiere ◽  
Cathy L. Miller

ABSTRACT Mammalian orthoreovirus (MRV) infection induces phosphorylation of translation initiation factor eIF2α, which promotes the formation of discrete cytoplasmic inclusions, termed stress granules (SGs). SGs are emerging as a component of the innate immune response to virus infection, and modulation of SG assembly is a common mechanism employed by viruses to counter this antiviral response. We previously showed that MRV infection induces SGs early and then interferes with SG formation as infection proceeds. In this work, we found that SG-associated proteins localized to the periphery of virus-encoded cytoplasmic structures, termed virus factories (VFs), where viral transcription, translation, and replication occur. The localization of SG proteins to VFs was dependent on polysome dissociation and occurred via association of the SG effector protein, Ras-GAP SH3-binding protein 1 (G3BP1), with the MRV nonstructural protein σNS, which localizes to VFs via association with VF nucleating protein, μNS. Deletion analysis of the σNS RNA binding domain and G3BP1 RNA (RRM) and ribosomal (RGG) binding domains showed that σNS association and VF localization phenotypes of G3BP1 do not occur solely through RNA or ribosomal binding but require both the RRM and RGG domains of G3BP1 for maximal viral-factory-like structure (VFL) localization and σNS association. Coexpression of σNS and μNS resulted in disruption of normal SG puncta, and in cells lacking G3BP1, MRV replication was enhanced in a manner correlating with strain-dependent induction of host translation shutoff. These results suggest that σNS association with G3BP1 and relocalization of G3BP1 to the VF periphery play roles in SG disruption to facilitate MRV replication in the host translational shutoff environment. IMPORTANCE SGs and SG effector proteins have emerged as important, yet poorly understood, players in the host's innate immune response to virus infection. MRV infection induces SGs early during infection that are dispersed and/or prevented from forming during late stages of infection despite continued activation of the eIF2α signaling pathway. Cellular and viral components involved in disruption of SGs during late stages of MRV infection remain to be elucidated. This work provides evidence that MRV disruption of SGs may be facilitated by association of the MRV nonstructural protein σNS with the major SG effector protein G3BP1 and subsequent localization of G3BP1 and other SG-associated proteins around the peripheries of virus-encoded factories, interrupting the normal formation of SGs. Our findings also reveal the importance of G3BP1 as an inhibitor of MRV replication during infection for the first time.


Immunology ◽  
2003 ◽  
Vol 110 (4) ◽  
pp. 519-526 ◽  
Author(s):  
Mark A. Exley ◽  
Nancy J. Bigley ◽  
Olivia Cheng ◽  
Angela Shaulov ◽  
Syed Muhammad Ali Tahir ◽  
...  

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