The Transmembrane Oligomers of Coronavirus Protein E

Torres, Jaume; Wang, Jifeng; Parthasarathy, Krupakar; Liu, Ding Xiang

doi:10.1529/biophysj.104.051730

Cited by 89 publications

(160 citation statements)

References 32 publications

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“…The SARS-CoV E protein forms homodimers and homotrimers under nonreducing conditions in E. coli [17]. The transmembrane domain (a.a. 9-35) of SARSCoV E protein forms SDS-resistant dimers, trimers, and pentamers [26]. The protein (about 18 kDa) that we detected was unglycosylated monomeric E protein with an unusual mobility on SDS-PAGE.…”

Section: Discussionmentioning

confidence: 69%

“…1B). Whether the second transmembrane region performs as the first one does in oligomer formation [26] and membrane permeabilization [16] needs further investigation. Figures 1 and 2 also imply that a nascent peptide of SARS-CoV E protein after the synthesis of the first or second transmembrane domains could integrate the peptide into the ER membrane, after which glycosylation occurs.…”

Section: Discussionmentioning

confidence: 99%

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Expression and membrane integration of SARS-CoV E protein and its interaction with M protein

Chen

et al. 2009

Virus Genes

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The severe acute respiratory syndrome (SARS)-CoV E gene fragment was cloned and expressed as a recombinant protein fused with a myc tag at the N-terminus in vitro and in Vero E6 cells. Similar to other N-glycosylated proteins, the glycosylation of SARS-CoV E protein occurred co-translationally in the presence of microsomes. The SARS-CoV E protein is predicted to be a double-spanning membrane protein lacking a conventional signal peptide. Both of the transmembrane regions (a.a. 11-33 and 37-59) are predicted to be alpha-helices, which penetrate into membranes by themselves. As expected, these two transmembrane regions inserted a cytoplasmic protein into the endoplasmic reticulum membrane. Either of these two transmembrane domains co-localized with M protein. Both the transmembrane domains of E protein are required to interact with M protein, while either of the hydrophilic regions (a.a. 1-10 or 60-76) is dispensable as shown by co-immunoprecipitation assay. These results are important for the study of SARS-CoV assembly.

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Section: Discussionmentioning

confidence: 69%

Section: Discussionmentioning

confidence: 99%

Expression and membrane integration of SARS-CoV E protein and its interaction with M protein

Chen

et al. 2009

Virus Genes

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“…As in other CoVs, the IBV E protein is a small structural protein containing a single hydrophobic domain with multiple functions [38][39][40][41][42] . Although information on the IBV E protein is limited [41,43] , those from different CoVs perform similar functions during viral infection [44] .…”

Section: Discussionmentioning

confidence: 99%

Genomic Characteristics and Changes of Avian Infectious Bronchitis Virus Strain CK/CH/LDL/97I after Serial Passages in Chicken Embryos

et al. 2014

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Background: We previously attenuated the infectious bronchitis virus (IBV) strain CK/CH/LDL/97I and found that it can convey protection against the homologous pathogenic virus. Objective: To compare the full-length genome sequences of the Chinese IBV strain CK/CH/LDL/97I and its embryo-passaged, attenuated level to identify sequence substitutions responsible for the attenuation and define markers of attenuation. Methods: The full-length genomes of CK/CH/LDL/97I P5 and P115 were amplified and sequenced. The sequences were assembled and compared using the MEGALIGN program (DNAStar) and a phylogenetic tree was constructed using MEGA4 software. Results: The CK/CH/LDL/97I virus population contained subpopulations with a mixture of genetic mutants. Changes were observed in nsp4, nsp9, nsp11/12, nsp14, nsp15, nsp16, and ORF3a, but these did not result in amino acid substitutions or did not show functional variations. Amino acid substitutions occurred in the remaining genes between P5 and P115; most were found in the S region, and some of the nucleotide mutations resulted in amino acid substitutions. Among the 9 nsps in the ORF1 region, nsp3 contained the most nucleotide substitutions. Conclusions: Sequence variations in different genes, especially the S gene and nsp3, in the genomes of CK/CH/LDL/97I viruses might contribute to differences in viral replication, pathogenicity, antigenicity, immunogenicity, and tissue tropism.

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“…44 A pentameric model was proposed that was later confirmed using infrared linear dichroism data from 13 …”

Section: Structure Of the Envelope Protein In Sars-covmentioning

confidence: 93%

Pentameric viral ion channels: from structure to function

Surya¹,

Li²,

Torres³

2014

JRLCR

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A family of small polypeptides in many virus types associate to form oligomers and have channel activity. These proteins have been referred to as viroporins or virochannels and are increasingly recognized as important virulence factors and potential drug targets. In this review, we focus on two of the viroporins that have been studied in more detail from a structural and functional point of view. One is the 76-residue envelope (E) protein found in coronaviruses (CoVs) that causes the severe acute respiratory syndrome (SARS). The other is the 65-residue small hydrophobic (SH) protein found in a paramyxovirus, the respiratory syncytial virus (RSV). RSV SH and SARS-CoV E proteins are short polypeptides with a single transmembrane domain. In both cases, the presence of the viroporin has a protective effect on cells, preventing early apoptosis, but it leads to increased virulence in infected animal models. Both viroporins form homopentameric oligomers that show channel activity with no or low selectivity. The role of channel activity is still unclear, but associations have been made to facilitation of the egress of the virus by modification of the secretory pathway, and contributions to inflammation. SARS-CoV E protein has a cytoplasmically oriented C-terminus and a lumenal N-terminus, whereas the opposite orientation is found in RSV SH protein. Despite this opposite topology, nuclear magnetic resonance (NMR)-based structural models of these two channels show a similar champagne flute shape, with the wider opening facing the cytoplasmic side. Good channel inhibitors are lacking, but those found seem to have a preference for the narrow end of the channel. Availability of good inhibitors will help reveal the specific role of these channels in the life cycle of these viruses.

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The Transmembrane Oligomers of Coronavirus Protein E

Cited by 89 publications

References 32 publications

Expression and membrane integration of SARS-CoV E protein and its interaction with M protein

Expression and membrane integration of SARS-CoV E protein and its interaction with M protein

Genomic Characteristics and Changes of Avian Infectious Bronchitis Virus Strain CK/CH/LDL/97I after Serial Passages in Chicken Embryos

Pentameric viral ion channels: from structure to function

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