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måndag 10 februari 2020

SARS-CoV ORF 6 funktiosta . Tekee interaktion nsp8:n kanssa,

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3219739/

Abstract Background
The ORF6 protein is one of the eight accessory proteins of the severe acute respiratory syndrome coronavirus (SARS-CoV). Numerous properties of ORF6 have been documented and this study focuses on two of these, namely, its ability to suppress the expression of co-transfected expression constructs and its subcellular localization to vesicular structures


Conclusions
By combining quantitative real-time PCR and transient transfection system, a simple and safe method is established to measure ORF6's ability to suppress the expression of co-transfected myc-nsp8. In addition, immunofluorescence analysis revealed that the subcellular localization of ORF6 when expressed on its own is similar to that observed in SARS-CoV infected cells. Through the use of these two assays, a putative diacidic motif in the ORF6 protein was found to influence its subcellular localization and ability to suppress the expression of co-transfected expression constructs.
Background
An outbreak of Severe Acute Respiratory Syndrome (SARS) in 2003 which carried with it a fatality rate of 8% was traced to a novel coronavirus dubbed the SARS Coronavirus (SARS-CoV). This novel coronavirus was eventually classified as a Group IIb coronavirus, a subset of the Group II coronaviruses. The subclassification was, in part, due to the presence of several accessory genes in the coronavirus which have no known homologs within the family Coronaviridae. These accessory genes have been the subject of study by many groups (for reviews, see 1 and 2) and have been assigned a plethora of physical characteristics and intracellular functions. Most importantly, almost all of these accessory genes have been shown to be dispensable for viral replication in cell culture, with the exception of the 3a accessory gene (3). It has been suggested these accessory genes have subtle effects on SARS-CoV replication and may be more important for viral replication or pathogenesis in vivo.
  • One of these accessory genes, ORF6, encodes for a ~7kDa protein with a hydrophobic N-terminal and that has been suggested to have a N-endo-C-endo conformation (4).
  •  Several groups have undertaken to characterize the protein product of the ORF6 gene and found that it interacts with the nsp8 protein from the SARS replicase complex (5),
  •  is able to increase infection titer during early infection at low multiplicity of infection (6), 
  • increase the rate of cellular gene synthesis (7), 
  • inhibit interferon production (8),
  •  and inhibit the nuclear translocation of STAT1 by interacting with karyopherin α2 (9). 
  • Most recently, the ORF6 protein has been suggested to induce intracellular membrane rearrangements resulting in a vesicular population in the infected cell which could possibly serve some role in increasing replication (10).
 Such virus-induced or virus associated vesicles have previously been shown in other viral infections, such as protein trafficking in Herpes simplex virus (11) and Sendai virus (12). Members of the coronavirus family have been shown by several groups to also utilize vesicular structures within the infected cell; most of these studies suggest that vesicles play a role in viral replication (13-16).
We have previously shown that the ORF6 protein colocalizes with Lamp1-positive vesicles in SARS-CoV infection (5) and also with the nsp8 protein in the same set of infected cells, indicating a possible role for the ORF6 protein in the replicative process of SARS-CoV.
 However, there has been, to date, little work done to link the subcellular localization of the ORF6 protein to its known functions. Gallagher and co-workers have shown that the ability of ORF6 to impede nuclear translocation resulted in the suppression of expression of transgenes from co-transfected expression constructs if these need transcription in the nucleus (17). Using this knowledge, a simple co-transfection system and alanine substitution mutants in the ORF6 gene are used here to determine regions of the ORF6 protein that modulate its ability to suppress the expression of co-transfected myc-nsp8. The subcellular localization of these mutants is then examined by immunofluorescence experiments and compared to that of wildtype ORF6.

(Kommentti:  ORF-kaavassa näyttää nCoV 2019 omaavat samantapaisen   ORF 6 :n) 

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