Subcellular Localization of SARS-CoV Structural Proteins

Lopez, Lisa A.; Jones, Ariel; Arndt, William; Hogue, Brenda G.

doi:10.1007/978-0-387-33012-9_51

Cited by 10 publications

(7 citation statements)

References 17 publications

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“…Strong transient expression of SARS-CoV E in the cis -Golgi, but hardly any expression in the ERGIC and trans-Golgi was also recently reported ( Cohen et al, 2011 , Nieto-Torres et al, 2011 , Teoh et al, 2010 ). We previously showed as well that HA-tagged SARS-CoV E localized in both the ERGIC and Golgi during transient expression ( Lopez et al, 2006 ). Collectively, it can be concluded that coronavirus E proteins are expressed in both ERGIC and Golgi compartments, though the distribution may vary depending on the virus and cell type.…”

Section: Discussionmentioning

confidence: 96%

Coronavirus envelope (E) protein remains at the site of assembly

et al. 2015

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Coronaviruses (CoVs) assemble at endoplasmic reticulum Golgi intermediate compartment (ERGIC) membranes and egress from cells in cargo vesicles. Only a few molecules of the envelope (E) protein are assembled into virions. The role of E in morphogenesis is not fully understood. The cellular localization and dynamics of mouse hepatitis CoV A59 (MHV) E protein were investigated to further understanding of its role during infection. E protein localized in the ERGIC and Golgi with the amino and carboxy termini in the lumen and cytoplasm, respectively. E protein does not traffic to the cell surface. MHV was genetically engineered with a tetracysteine tag at the carboxy end of E. Fluorescence recovery after photobleaching (FRAP) showed that E is mobile in ERGIC/Golgi membranes. Correlative light electron microscopy (CLEM) confirmed the presence of E in Golgi cisternae. The results provide strong support that E proteins carry out their function(s) at the site of budding/assembly.

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Section: Discussionmentioning

confidence: 96%

Coronavirus envelope (E) protein remains at the site of assembly

et al. 2015

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“…Other groups have examined the expression of epitope-tagged SARS-CoV E protein and reported its localization in the ER, ERGIC, or Golgi complex (1,27,30,35,51). To investigate the targeting of untagged SARS-CoV E protein to Golgi membranes, we expressed SARS-CoV E from cDNA in HeLa cells and examined its localization by indirect immunofluorescence microscopy.…”

Section: The Sars-cov E Protein Is Targeted To the Golgi Regionmentioning

confidence: 99%

“…At least two different membrane topologies of SARS-CoV E have been reported: single spanning and membrane hairpin (3,40,51). When expressed from cDNA, epitope-tagged SARS-CoV E protein was reported to localize to the endoplasmic reticulum (ER), ERGIC, or Golgi complex (1,26,30,46).…”

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confidence: 99%

Identification of a Golgi Complex-Targeting Signal in the Cytoplasmic Tail of the Severe Acute Respiratory Syndrome Coronavirus Envelope Protein

Cohen

Lin

Machamer

2011

J Virol

125

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The 2003 global outbreak of progressive respiratory failure was caused by a newly emerged virus, severe acute respiratory syndrome coronavirus (SARS-CoV). In contrast to many well-studied enveloped viruses that assemble and bud at the plasma membrane, coronaviruses assemble by budding into the lumen of the endoplasmic reticulum-Golgi intermediate compartment and are released from the cell by exocytosis. For this to occur, the viral envelope proteins must be efficiently targeted to the Golgi region of the secretory pathway. Although the envelope protein (E) makes up only a small percentage of the viral envelope, it plays an important, as-yet-undefined role in virus production. To dissect the targeting of the SARS-CoV E protein to the Golgi region, we exogenously expressed the protein and various mutants from cDNA and determined their localization using immunofluorescence microscopy and biochemical assays. We show that the cytoplasmic tail of the SARS-CoV E protein is sufficient to redirect a plasma membrane protein to the Golgi region. Through site-directed mutagenesis, we demonstrate that a predicted beta-hairpin structural motif in the tail is sufficient for Golgi complex localization of a reporter protein. This motif is conserved in E proteins of beta and gamma coronaviruses (formerly referred to as group 2 and 3 coronaviruses), where it also functions as a Golgi complex-targeting signal. Dissecting the mechanism of targeting of the SARS-CoV E protein will lead to a better understanding of its role in the assembly and release of virions.

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“…CoV E proteins (76-109 amino acids in length) also adopt a predominantly N exo -C endo topology in the membrane ( Fig. 3a) (Ruch and Machamer 2012b;Corse and Machamer 2000;Nieto-Torres et al 2011) and are targeted to the Golgi region in infected and transfected cells (Corse and Machamer 2000;Lopez et al 2006;Raamsman et al 2000;Liao et al 2006). Synthetic peptides corresponding to full-length E proteins from four different coronaviruses demonstrated cation-specific currents in planar bilayers (Wilson et al 2004;Wilson et al 2006).…”

Section: The Cov E Protein and Virus Egressmentioning

confidence: 99%

Accommodation of large cargo within Golgi cisternae

Machamer

2013

Histochem Cell Biol

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In mammalian cells, the Golgi complex has an elaborate structure consisting of stacked, flattened cisternal membranes collected into a ribbon in the center of the cell. Amazingly, the flattened cisternae can rapidly dilate to accommodate large cargo as it traffics through the organelle. The mechanism by which this occurs is unknown. Exocytosis of large cargo is essential for many physiological processes, including collagen and lipoprotein secretion, and defects in the process lead to disease. In addition, enveloped viruses that bud into the endoplasmic reticulum or Golgi complex must also be transported through Golgi cisternae for secretion from the infected cell. This review summarizes our understanding of intra-Golgi transport of large cargo, and outlines current questions open for experimentation.

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Subcellular Localization of SARS-CoV Structural Proteins

Cited by 10 publications

References 17 publications

Coronavirus envelope (E) protein remains at the site of assembly

Coronavirus envelope (E) protein remains at the site of assembly

Identification of a Golgi Complex-Targeting Signal in the Cytoplasmic Tail of the Severe Acute Respiratory Syndrome Coronavirus Envelope Protein

Accommodation of large cargo within Golgi cisternae

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