Crimean-Congo Hemorrhagic Fever Virus-Infected Hepatocytes Induce ER-Stress and Apoptosis Crosstalk

Rodrigues, Renata; Paranhos-Baccalà, Gláucia; Vernet, Guy; Peyrefitte, Christophe N.

doi:10.1371/journal.pone.0029712

Cited by 65 publications

(60 citation statements)

References 67 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These time points correlate with high levels of progeny virus production and release from the host cells. Apoptosis-inducing viruses of the family Bunyaviridae like Oropouche virus, Crimean-Congo hemorrhagic fever virus or hantavirus show comparable time-courses for the induction of apoptosis (Acrani et al, 2010;Karlberg et al, 2011), and for these viruses it was shown that apoptosis of the host cell was not induced by binding or entry of the virus but by viral replication (Acrani et al, 2010;Li et al, 2004;Rodrigues et al, 2012). Similarly, experiments with UV-inactivated viruses such as West Nile virus, Newcastle disease virus, Oropouche virus and enterovirus have also identified a dependence on viral replication as the major apoptosis-inducing factor (Acrani et al, 2010;Kleinschmidt et al, 2007;Ravindra et al, 2008;Shih et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

“…For many viruses, like SeV, West Nile virus, Crimean-Congo hemorrhagic fever virus, simian varicella virus, transmissible gastroenteritis virus or human astrovirus, it has been demonstrated that infection of the host cell can lead to activation of both caspases 8 and 9 and their associated signal transduction pathways (Banos-Lara & Méndez, 2010;Bitzer et al, 1999Bitzer et al, , 2002Eleouet et al, 1998;Kleinschmidt et al, 2007;Pugazhenthi et al, 2009;Rodrigues et al, 2012). The exact mechanism(s) by which these signalling pathways are activated during TCRV infection, and which cellular factors are involved, remain to be analysed.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

The New World arenavirus Tacaribe virus induces caspase-dependent apoptosis in infected cells

Wolff

Groseth

Meyer

et al. 2016

Journal of General Virology

View full text Add to dashboard Cite

The Arenaviridae is a diverse and growing family of viruses that already includes more than 25 distinct species. While some of these viruses have a significant impact on public health, others appear to be non-pathogenic. At present little is known about the host cell responses to infection with different arenaviruses, particularly those found in the New World; however, apoptosis is known to play an important role in controlling infection of many viruses. Here we show that infection with Tacaribe virus (TCRV), which is widely considered the prototype for non-pathogenic arenaviruses, leads to stronger induction of apoptosis than does infection with its human-pathogenic relative Junín virus. TCRV-induced apoptosis occurred in several cell types during late stages of infection and was shown to be caspase-dependent, involving the activation of caspases 3, 7, 8 and 9. Further, UV-inactivated TCRV did not induce apoptosis, indicating that the activation of this process is dependent on active viral replication/transcription. Interestingly, when apoptosis was inhibited, growth of TCRV was not enhanced, indicating that apoptosis does not have a direct negative effect on TCRV infection in vitro. Taken together, our data identify and characterize an important virus-host cell interaction of the prototypic, non-pathogenic arenavirus TCRV, which provides important insight into the growing field of arenavirus research aimed at better understanding the diversity in responses to different arenavirus infections and their functional consequences.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

The New World arenavirus Tacaribe virus induces caspase-dependent apoptosis in infected cells

Wolff

Groseth

Meyer

et al. 2016

Journal of General Virology

View full text Add to dashboard Cite

show abstract

“…CCHFV replication in cell culture results in the induction of apoptosis at late time points within the infectious cycle (40), and the onset of apoptosis coincides with cleavage of the N protein by cellular caspase-3, at a conserved DEVD motif at residues 269 to 272 (19).…”

Section: ) (C)mentioning

confidence: 99%

Structure, Function, and Evolution of the Crimean-Congo Hemorrhagic Fever Virus Nucleocapsid Protein

Carter

Surtees

Walter

et al. 2012

J Virol

105

131

View full text Add to dashboard Cite

c Crimean-Congo hemorrhagic fever virus (CCHFV) is an emerging tick-borne virus of the Bunyaviridae family that is responsible for a fatal human disease for which preventative or therapeutic measures do not exist. We solved the crystal structure of the CCHFV strain Baghdad-12 nucleocapsid protein (N), a potential therapeutic target, at a resolution of 2.1 Å. N comprises a large globular domain composed of both N-and C-terminal sequences, likely involved in RNA binding, and a protruding arm domain with a conserved DEVD caspase-3 cleavage site at its apex. Alignment of our structure with that of the recently reported N protein from strain YL04057 shows a close correspondence of all folds but significant transposition of the arm through a rotation of 180 degrees and a translation of 40 Å. These observations suggest a structural flexibility that may provide the basis for switching between alternative N protein conformations during important functions such as RNA binding and oligomerization. Our structure reveals surfaces likely involved in RNA binding and oligomerization, and functionally critical residues within these domains were identified using a minigenome system able to recapitulate CCHFV-specific RNA synthesis in cells. Caspase-3 cleaves the polypeptide chain at the exposed DEVD motif; however, the cleaved N protein remains an intact unit, likely due to the intimate association of N-and C-terminal fragments in the globular domain. Structural alignment with existing N proteins reveals that the closest CCHFV relative is not another bunyavirus but the arenavirus Lassa virus instead, suggesting that current segmented negative-strand RNA virus taxonomy may need revision.

show abstract

“…PUMA-dependent induction of PCD is reported after bacterial and viral infections [65][66][67]. Recently, an increased expression of PUMA and NOXA has been described in gastric epithelial cells infected with Helicobacter pylori [65].…”

Section: Immune Modulation Infectionsmentioning

confidence: 99%

Puma, a critical mediator of cell death — one decade on from its discovery

Hikisz

Kiliańska

2012

Cellular and Molecular Biology Letters

105

View full text Add to dashboard Cite

Abbreviations used: ADI/II -activation domain I/II; Apaf-1 -apoptosis protease activating factor-1; Bad -Bcl-2 associated death promoter; Bak -Bcl-2 antagonist killer; Bax -Bcl-2 associated protein x; Bcl-2 -B-cell leukemia/lymphoma-2; BH1-4 -Bcl-2 homology domains 1-4; Bid -BH3 interacting domain death agonist; Bik -Bcl-2 interacting killer; Bim -Bcl-2 interacting mediator of cell death; Bmf -Bcl-2 modifying factor; Bod -Bcl-2-related ovarian death gene; Bok -Bcl-2 ovarian killer; BS1/2 -p53 binding site 1/2; CHOP -C/EBP homologous protein; DEN -diethylnitrosamine; GSK-3 -glycogen synthase kinase-3; HRK -harakiri, activator of apoptosis ; HSPCs -hematopoietic stem/progenitor cells; HSV-1 -human herpes virus; IKK -IκB kinase; IL-3 -interleukin 3; Lys -lysine; Mcl-1 -myeloid cell leukemia-1; MEFs -mouse embryo fibroblasts; miRNA/miR -microRNA; MLS -mitochondrial localization signal; MOMPmitochondrial outer membrane permeabilization; NOXA (PMAP1) -phorbol-12-myristate-13-acetate-induced protein 1; OMM -outer mitochondrial membrane; PCDprogrammed cell death; PI3K -phosphoinositide 3-kinase; PUMA -p53 upregulated modulator of apoptosis; ROS -reactive oxygen species; Ser -serine; Smac/DIABLOsecond mitochondria-derived activator or caspases/direct IAP binding protein with low pI; TRB3 -tribbles 3 homolog; UV-IR -ultraviolet-gamma irradiation Abstract: PUMA (p53 upregulated modulator of apoptosis) is a pro-apoptotic member of the BH3-only subgroup of the Bcl-2 family. It is a key mediator of p53-dependent and p53-independent apoptosis and was identified 10 years ago. The PUMA gene is mapped to the long arm of chromosome 19, a region that is frequently deleted in a large number of human cancers. PUMA mediates apoptosis thanks to its ability to directly bind known anti-apoptotic members of the Bcl-2 family. It mainly localizes to the mitochondria. The binding of PUMA to the inhibitory members of the Bcl-2 family (Bcl-2-like proteins) via its BH3 domain seems to be a critical regulatory step in the induction of apoptosis. It results in the displacement of the proteins Bax and/or Bak. This is followed by their activation and the formation of pore-like structures on the mitochondrial Unauthenticated Download Date | 5/11/18 3:27 AM CELLULAR & MOLECULAR BIOLOGY LETTERS 647 membrane, which permeabilizes the outer mitochondrial membrane, leading to mitochondrial dysfunction and caspase activation. PUMA is involved in a large number of physiological and pathological processes, including the immune response, cancer, neurodegenerative diseases and bacterial and viral infections.

show abstract

Crimean-Congo Hemorrhagic Fever Virus-Infected Hepatocytes Induce ER-Stress and Apoptosis Crosstalk

Cited by 65 publications

References 67 publications

The New World arenavirus Tacaribe virus induces caspase-dependent apoptosis in infected cells

The New World arenavirus Tacaribe virus induces caspase-dependent apoptosis in infected cells

Structure, Function, and Evolution of the Crimean-Congo Hemorrhagic Fever Virus Nucleocapsid Protein

Puma, a critical mediator of cell death — one decade on from its discovery

Contact Info

Product

Resources

About