SARS Coronavirus E Protein in Phospholipid Bilayers: An X-Ray Study

Khattari, Z. Y.; Brotons, Guillaume; Akkawi, Mutaz; Arbely, Eyal; Arkin, Isaiah T.; Salditt, Tim

doi:10.1529/biophysj.105.072892

Cited by 35 publications

(42 citation statements)

References 46 publications

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“…We note that our results are in general inconsistent with previous reports (23,45) that suggest that ETM forms a membrane-destabilizing, totally embedded, a-helical transmembrane hairpin. Indeed, we show by DLS that ETM has no disturbing effect on lipid bilayers, and does not induce tubular morphologies.…”

Section: Discussioncontrasting

confidence: 99%

Model of a Putative Pore: The Pentameric α-Helical Bundle of SARS Coronavirus E Protein in Lipid Bilayers

Torres

Parthasarathy

Lin

et al. 2006

Biophysical Journal

106

131

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The coronavirus responsible for the severe acute respiratory syndrome contains a small envelope protein, E, with putative involvement in host apoptosis and virus morphogenesis. To perform these functions, it has been suggested that protein E can form a membrane destabilizing transmembrane (TM) hairpin, or homooligomerize to form a TM pore. Indeed, in a recent study we reported that the alpha-helical putative transmembrane domain of E protein (ETM) forms several SDS-resistant TM interactions: a dimer, a trimer, and two pentameric forms. Further, these interactions were found to be evolutionarily conserved. Herein, we have studied multiple isotopically labeled ETM peptides reconstituted in model lipid bilayers, using the orientational parameters derived from infrared dichroic data. We show that the topology of ETM is consistent with a regular TM alpha-helix. Further, the orientational parameters obtained unequivocally correspond to a homopentameric model, by comparison with previous predictions. We have independently confirmed that the full polypeptide of E protein can also aggregate as pentamers after expression in Escherichia coli. This interaction must be stabilized, at least partially, at the TM domain. The model we report for this pentameric alpha-helical bundle may explain some of the permabilizing properties of protein E, and should be the basis of mutagenesis efforts in future functional studies.

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Section: Discussioncontrasting

confidence: 99%

Model of a Putative Pore: The Pentameric α-Helical Bundle of SARS Coronavirus E Protein in Lipid Bilayers

Torres

Parthasarathy

Lin

et al. 2006

Biophysical Journal

106

131

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“…The 3′ end of PEDV genome containing four structural proteins (S, E, M and N) and one nonstructural protein (ORF3) plays an important role during RNA binding after phosphorylation, virus assembly, immunogenic activity and virulence (de Haan et al, 1998). The E protein, a small transmembrane protein of 76 to 109 amino acids in length, plays a pivotal role in the assembly of virions by inducing membrane curvature or aid in membrane scission (Fischer et al, 1998;Khattari et al, 2006). In addition, the E protein has ion channel activity and interacts with host proteins Pervushin et al, 2009;Teoh et al, 2010;Wilson et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

Evolutionary characterization of the emerging porcine epidemic diarrhea virus worldwide and 2014 epidemic in Taiwan

Sung

Deng

Chung

et al. 2015

Infection, Genetics and Evolution

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Since 2010, a new variant of PEDV belonging to Genogroup 2 has been transmitting in China and further spreading to the Unites States and other Asian countries including Taiwan. In order to characterize in detail the temporal and geographic relationships among PEDV strains, the present study systematically evaluated the evolutionary patterns and phylogenetic resolution in each gene of the whole PEDV genome in order to determine which regions provided the maximal interpretative power. The result was further applied to identify the origin of PEDV that caused the 2014 epidemic in Taiwan. Thirty-four full genome sequences were downloaded from GenBank and divided into three non-mutually exclusive groups, namely, worldwide, Genogroup 2 and China, to cover different ranges of secular and spatial trends. Each dataset was then divided into different alignments by different genes for likelihood mapping and phylogenetic analysis. Our study suggested that both nsp3 and S genes contained the highest phylogenetic signal with substitution rate and phylogenetic topology similar to those obtained from the complete genome. Furthermore, the proportion of nodes with high posterior support (posterior probability >0.8) was similar between nsp3 and S genes. The nsp3 gene sequences from three clinical samples of swine with PEDV infections were aligned with other strains available from GenBank and the results suggested that the virus responsible for the 2014 PEDV outbreak in Taiwan clustered together with Clade I from the US within Genogroup 2. In conclusion, the current study identified the nsp3 gene as an alternative marker for a rapid and unequivocal classification of the circulating PEDV strains which provides complementary information to the S gene in identifying the emergence of epidemic strain resulting from recombination.

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“…The MHV E protein has been reported to have both the C-terminus (Maeda et al, 2001;Raamsman et al, 2000) and its N-terminus (Maeda et al, 2001) oriented toward the cytoplasm in a hairpin-like topology. Two different topologies have been reported for the SARS protein, one a hairpin topology with both the N-and C-termini oriented toward the cytoplasm (Arbely et al, 2004;Khattari et al, 2005;Yuan et al, 2006a), and a second topology with a single membrane-spanning domain with the Cterminus in the cytoplasm and the N-terminus oriented toward the lumen (Nieto- Torres et al, 2011;Yuan et al, 2006a).…”

Section: B Small Membrane (E) Proteinmentioning

confidence: 99%