The 8ab protein of SARS-CoV is a luminal ER membrane-associated protein and induces the activation of ATF6

Sung, Shu-Chiun; Chao, Che‐Yi; Jeng, King‐Song; Yang, Pan‐Chyr; Lai, Michael M. C.

doi:10.1016/j.virol.2009.02.021

Cited by 97 publications

(116 citation statements)

References 45 publications

(72 reference statements)

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“…The mature p8ab remains associated with the ER and possibly undergoes multimerization, but it is not transported to the Golgi for secretion (Oostra et al, 2007). Inside the ER, the protein up-regulates the synthesis of ER chaperons and activates the ATF6 branch of unfolded-protein response (UPR), but shows no effect on the PERK and IRE1 branches of the UPR (Sung et al, 2009). The 29-nt deletion disrupts the functional expression of ORF8.…”

Section: Sars-cov P7bmentioning

confidence: 99%

Accessory proteins of SARS-CoV and other coronaviruses

et al. 2014

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The huge RNA genome of SARS coronavirus comprises a number of open reading frames that code for a total of eight accessory proteins. Although none of these are essential for virus replication, some appear to have a role in virus pathogenesis. Notably, some SARS-CoV accessory proteins have been shown to modulate the interferon signaling pathways and the production of pro-inflammatory cytokines. The structural information on these proteins is also limited, with only two (p7a and p9b) having their structures determined by X-ray crystallography. This review makes an attempt to summarize the published knowledge on SARS-CoV accessory proteins, with an emphasis on their involvement in virus-host interaction. The accessory proteins of other coronaviruses are also briefly discussed. This paper forms part of a series of invited articles in Antiviral Research on "From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses" (see Introduction by Hilgenfeld and Peiris (2013)).

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Section: Sars-cov P7bmentioning

confidence: 99%

Accessory proteins of SARS-CoV and other coronaviruses

et al. 2014

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“…Interestingly, a HCoV-OC43 variant harboring persistence-associated mutations in the spike protein has been found to induce a stronger ER stress and UPR in the infected neurons as compared to the wild type virus (Favreau et al, 2009). Apart from the spike protein, some coronavirus accessory proteins, such as protein 3a, 6 and 8ab of SARS-CoV, have also been shown to induced ER stress when over-expressed in cells (Minakshi et al, 2009;Sung et al, 2009;Ye et al, 2008).…”

Section: Coronavirus Proteins and Er Stressmentioning

confidence: 99%

“…Overexpression of the SARS-CoV spike protein also fails to activate ATF6 reporter constructs (Chan et al, 2006). In contrast, ATF6 cleavage and nuclear translocation have been determined in cells transfected with the SARS-CoV accessory protein 8ab, which has also been shown to physically interact with the luminal domain of ATF6 (Sung et al, 2009). The SARS-CoV 8ab protein was only detected in early human isolates during the SARS-CoV pandemic.…”

Section: Activation Of Atf6 Pathway During Coronavirus Infectionmentioning

confidence: 99%

Coronavirus-induced ER stress response and its involvement in regulation of coronavirus–host interactions

2014

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Coronavirus replication is structurally and functionally associated with the endoplasmic reticulum (ER), a major site of protein synthesis, folding, modification and sorting in the eukaryotic cells. Disturbance of ER homeostasis may occur under various physiological or pathological conditions. In response to the ER stress, signaling pathways of the unfolded protein response (UPR) are activated. UPR is mediated by three ER transmembrane sensors, namely the PKR-like ER protein kinase (PERK), the inositol-requiring protein 1 (IRE1) and the activating transcriptional factor 6 (ATF6). UPR facilitates adaptation to ER stress by reversible translation attenuation, enhancement of ER protein folding capacity and activation of ER-associated degradation (ERAD). In cells under prolonged and irremediable ER stress, UPR can also trigger apoptotic cell death. Accumulating evidence has shown that coronavirus infection causes ER stress and induces UPR in the infected cells. UPR is closely associated with a number of major signaling pathways, including autophagy, apoptosis, the mitogen-activated protein (MAP) kinase pathways, innate immunity and pro-inflammatory response. Therefore, studies on the UPR are pivotal in elucidating the complicated issue of coronavirus-host interaction. In this paper, we present the up-to-date knowledge on coronavirus-induced UPR and discuss its potential involvement in regulation of innate immunity and apoptosis.

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“…Interestingly, this difference is due to a 29 nucleotide deletion in the mRNA8 of SARS-CoV from some animal species [110,111,112,113,114], that splits ORF 8 into ORF8a and ORF8b, encoding 39- and 84-residue polypeptides, respectively [110]. In fact, larger deletions were reported in sequenced ORF8 genes from a cluster of viruses that were isolated from humans later during the SARS epidemic [111,115].…”

Section: Sars Accessory Proteinsmentioning

confidence: 99%

The Role of Severe Acute Respiratory Syndrome (SARS)-Coronavirus Accessory Proteins in Virus Pathogenesis

McBride

Fielding

2012

Viruses

137

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A respiratory disease caused by a novel coronavirus, termed the severe acute respiratory syndrome coronavirus (SARS-CoV), was first reported in China in late 2002. The subsequent efficient human-to-human transmission of this virus eventually affected more than 30 countries worldwide, resulting in a mortality rate of ~10% of infected individuals. The spread of the virus was ultimately controlled by isolation of infected individuals and there has been no infections reported since April 2004. However, the natural reservoir of the virus was never identified and it is not known if this virus will re-emerge and, therefore, research on this virus continues. The SARS-CoV genome is about 30 kb in length and is predicted to contain 14 functional open reading frames (ORFs). The genome encodes for proteins that are homologous to known coronavirus proteins, such as the replicase proteins (ORFs 1a and 1b) and the four major structural proteins: nucleocapsid (N), spike (S), membrane (M) and envelope (E). SARS-CoV also encodes for eight unique proteins, called accessory proteins, with no known homologues. This review will summarize the current knowledge on SARS-CoV accessory proteins and will include: (i) expression and processing; (ii) the effects on cellular processes; and (iii) functional studies.

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The 8ab protein of SARS-CoV is a luminal ER membrane-associated protein and induces the activation of ATF6

Cited by 97 publications

References 45 publications

Accessory proteins of SARS-CoV and other coronaviruses

Accessory proteins of SARS-CoV and other coronaviruses

Coronavirus-induced ER stress response and its involvement in regulation of coronavirus–host interactions

The Role of Severe Acute Respiratory Syndrome (SARS)-Coronavirus Accessory Proteins in Virus Pathogenesis

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