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Coronavirus envelope protein

January 20, 2023

The envelope (E) protein is the smallest and least well-characterized of the four major structural proteins found in coronavirus virions.[2][3][4] It is an integral membrane protein less than 110 amino acid residues long;[2] in SARS-CoV-2, the causative agent of Covid-19, the E protein is 75 residues long.[5] Although it is not necessarily essential for viral replication, absence of the E protein may produce abnormally assembled viral capsids or reduced replication.[2][3] E is a multifunctional protein[6] and, in addition to its role as a structural protein in the viral capsid, it is thought to be involved in viral assembly, likely functions as a viroporin, and is involved in viral pathogenesis.[2][5]

Envelope protein
Model of the external structure of the SARS-CoV-2 virion.[1]
● Blue: envelope
● Turquoise: spike glycoprotein (S)
● Red: envelope proteins (E)
● Green: membrane proteins (M)
● Orange: glycans
Identifiers
SymbolCoV_E
PfamPF02723
InterProIPR003873
PROSITEPS51926
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Structure

 
Solid-state NMR structure of the pentameric pore formed by the transmembrane helices of the SARS-CoV-2 E protein, which forms a viroporin permeable to cations.[5][4] Rendered from PDB: 7K3G​.

The E protein consists of a short hydrophilic N-terminal region, a hydrophobic helical transmembrane domain, and a somewhat hydrophilic C-terminal region. In SARS-CoV and SARS-CoV-2, the C-terminal region contains a PDZ domain binding motif (PBM).[2][5] This feature appears to be conserved only in the alpha and beta coronavirus groups, but not gamma.[2] In the beta and gamma groups, a conserved proline residue is found in the C-terminal region likely involved in targeting the protein to the Golgi.[2]

The transmembrane helices of the E proteins of SARS-CoV and SARS-CoV-2 can oligomerize and have been shown in vitro to form pentameric structures with central pores that serve as cation-selective ion channels.[5] Both viruses' E protein pentamers have been structurally characterized by nuclear magnetic resonance spectroscopy.[5][7]

The membrane topology of the E protein has been studied in a number of coronaviruses with inconsistent results; the protein's orientation in the membrane may be variable.[3] The balance of evidence suggests the most common orientation has the C-terminus oriented toward the cytoplasm.[8] Studies of SARS-CoV-2 E protein are consistent with this orientation.[5][9]

Post-translational modifications

In some, but not all, coronaviruses, the E protein is post-translationally modified by palmitoylation on conserved cysteine residues.[2][8] In the SARS-CoV E protein, one glycosylation site has been observed, which may influence membrane topology;[8] however, the functional significance of E glycosylation is unclear.[2] Ubiquitination of SARS-CoV E has also been described, though its functional significance is also not known.[2]

Expression and localization

Genomic information
 
Genomic organisation of isolate Wuhan-Hu-1, the earliest sequenced sample of SARS-CoV-2, indicating the location of the E gene
NCBI genome ID86693
Genome size29,903 bases
Year of completion2020
Genome browser (UCSC)

The E protein is expressed at high abundance in infected cells. However, only a small amount of the total E protein produced is found in assembled virions.[2][4] E protein is localized to the endoplasmic reticulum, Golgi apparatus, and endoplasmic-reticulum–Golgi intermediate compartment (ERGIC), the intracellular compartment that gives rise to the coronavirus viral envelope.[2][5]

Function

Essentiality

Studies in different coronaviruses have reached different conclusions about whether E is essential to viral replication. In some coronaviruses, including MERS-CoV, E has been reported to be essential.[10] In others, including mouse coronavirus[11] and SARS-CoV, E is not essential, though its absence reduces viral titer,[12] in some cases by introducing propagation defects or causing abnormal capsid morphology.[2]

Virions and viral assembly

 
Illustration of a coronavirus virion in the respiratory mucosa, showing the positions of the four structural proteins and components of the extracellular environment.[13]

The E protein is found in assembled virions where it forms protein-protein interactions with the coronavirus membrane protein (M), the most abundant of the four structural proteins contained in the viral capsid.[2][4] The interaction between E and M occurs through their respective C-termini on the cytoplasmic side of the membrane.[2] In most coronaviruses, E and M are sufficient to form virus-like particles,[2][4] though SARS-CoV has been reported to depend on N as well.[14] There is good evidence that E is involved in inducing membrane curvature to create the typical spherical coronavirus virion.[2][15] It is likely that E is involved in viral budding or scission, although its role in this process has not been well characterized.[2][4][15]

Viroporin

In its pentameric state, E forms cation-selective ion channels and likely functions as a viroporin.[5] This may disrupt ion homeostasis, alter membrane permeability, and modulate pH in the host cell, which may facilitate viral release.[2][4] The E protein's role as a viroporin appears to be involved in pathogenesis and may be related to activation of the inflammasome.[3][16] In SARS-CoV, mutations that disrupt E's ion channel function result in attenuated pathogenesis in animal models despite little effect on viral growth.[10]

Interactions with host proteins

 
Cryo-electron microscopy structure of the interaction between the SARS-CoV-2 E protein PDZ-binding motif (magenta) and a construct containing the PDZ (blue), SH3 (yellow), and guanylate kinase-like (GK, green) domains from a host cell protein, human PALS1.[17]

Protein-protein interactions between E and proteins in the host cell are best described in SARS-CoV and occur via the C-terminal PDZ domain binding motif. The SARS-CoV E protein has been reported to interact with five host cell proteins: Bcl-xL, PALS1, syntenin, sodium/potassium (Na+/K+) ATPase α-1 subunit, and stomatin.[2] The interaction with PALS1 may be related to pathogenesis via the resulting disruption in tight junctions.[3][10] This interaction has also been identified in SARS-CoV-2.[17]

Evolution and conservation

The sequence of the E protein is not well conserved across coronavirus genera, with sequence identities reaching under 30%.[12] In laboratory experiments on mouse hepatitis virus, substitution of E proteins from different coronaviruses, even from different groups, could produce viable viruses, suggesting that significant sequence diversity can be tolerated in functional E proteins.[18] The SARS-CoV-2 E protein is very similar to that of SARS-CoV, with three substitutions and one deletion.[4] A study of SARS-CoV-2 sequences suggests that the E protein is evolving relatively slowly compared to other structural proteins.[19] The conserved nature of the envelope protein among SARS-CoV and SARS-CoV-2 variants has led it to be researched as a potential target for universal coronavirus vaccine development.[20][21]

References

  1. ^ Solodovnikov, Alexey; Arkhipova, Valeria (2021-07-29). [Truly beautiful: how we made the SARS-CoV-2 3D model] (in Russian). N+1. Archived from the original on 2021-07-30. Retrieved 30 July 2021.
  2. ^ a b c d e f g h i j k l m n o p q r s t Schoeman, Dewald; Fielding, Burtram C. (December 2019). "Coronavirus envelope protein: current knowledge". Virology Journal. 16 (1): 69. doi:10.1186/s12985-019-1182-0. PMC 6537279. PMID 31133031.
  3. ^ a b c d e Schoeman, Dewald; Fielding, Burtram C. (2020-09-03). "Is There a Link Between the Pathogenic Human Coronavirus Envelope Protein and Immunopathology? A Review of the Literature". Frontiers in Microbiology. 11: 2086. doi:10.3389/fmicb.2020.02086. PMC 7496634. PMID 33013759.
  4. ^ a b c d e f g h Cao, Yipeng; Yang, Rui; Lee, Imshik; Zhang, Wenwen; Sun, Jiana; Wang, Wei; Meng, Xiangfei (June 2021). "Characterization of the SARS‐CoV ‐2 E Protein: Sequence, Structure, Viroporin, and Inhibitors". Protein Science. 30 (6): 1114–1130. doi:10.1002/pro.4075. ISSN 0961-8368. PMC 8138525. PMID 33813796.
  5. ^ a b c d e f g h i Mandala, Venkata S.; McKay, Matthew J.; Shcherbakov, Alexander A.; Dregni, Aurelio J.; Kolocouris, Antonios; Hong, Mei (December 2020). "Structure and drug binding of the SARS-CoV-2 envelope protein transmembrane domain in lipid bilayers". Nature Structural & Molecular Biology. 27 (12): 1202–1208. doi:10.1038/s41594-020-00536-8. PMC 7718435. PMID 33177698.
  6. ^ Liu, D. X.; Yuan, Q.; Liao, Y. (August 2007). "Coronavirus envelope protein: A small membrane protein with multiple functions". Cellular and Molecular Life Sciences. 64 (16): 2043–2048. doi:10.1007/s00018-007-7103-1. PMC 7079843. PMID 17530462.
  7. ^ Surya, Wahyu; Li, Yan; Torres, Jaume (June 2018). "Structural model of the SARS coronavirus E channel in LMPG micelles". Biochimica et Biophysica Acta (BBA) - Biomembranes. 1860 (6): 1309–1317. doi:10.1016/j.bbamem.2018.02.017. PMC 7094280. PMID 29474890.
  8. ^ a b c Fung, To Sing; Liu, Ding Xiang (June 2018). "Post-translational modifications of coronavirus proteins: roles and function". Future Virology. 13 (6): 405–430. doi:10.2217/fvl-2018-0008. PMC 7080180. PMID 32201497.
  9. ^ Duart, Gerard; García-Murria, Mª Jesús; Grau, Brayan; Acosta-Cáceres, José M.; Martínez-Gil, Luis; Mingarro, Ismael (September 2020). "SARS-CoV-2 envelope protein topology in eukaryotic membranes". Open Biology. 10 (9): 200209. doi:10.1098/rsob.200209. PMC 7536074. PMID 32898469.
  10. ^ a b c DeDiego, Marta L.; Nieto-Torres, Jose L.; Jimenez-Guardeño, Jose M.; Regla-Nava, Jose A.; Castaño-Rodriguez, Carlos; Fernandez-Delgado, Raul; Usera, Fernando; Enjuanes, Luis (December 2014). "Coronavirus virulence genes with main focus on SARS-CoV envelope gene". Virus Research. 194: 124–137. doi:10.1016/j.virusres.2014.07.024. PMC 4261026. PMID 25093995.
  11. ^ Kuo, Lili; Masters, Paul S. (2003-04-15). "The Small Envelope Protein E Is Not Essential for Murine Coronavirus Replication". Journal of Virology. 77 (8): 4597–4608. doi:10.1128/JVI.77.8.4597-4608.2003. PMC 152126. PMID 12663766.
  12. ^ a b Ruch, Travis R.; Machamer, Carolyn E. (2012-03-08). "The Coronavirus E Protein: Assembly and Beyond". Viruses. 4 (3): 363–382. doi:10.3390/v4030363. PMC 3347032. PMID 22590676.
  13. ^ Goodsell, David S.; Voigt, Maria; Zardecki, Christine; Burley, Stephen K. (6 August 2020). "Integrative illustration for coronavirus outreach". PLOS Biology. 18 (8): e3000815. doi:10.1371/journal.pbio.3000815. PMC 7433897. PMID 32760062.
  14. ^ Siu, Y. L.; Teoh, K. T.; Lo, J.; Chan, C. M.; Kien, F.; Escriou, N.; Tsao, S. W.; Nicholls, J. M.; Altmeyer, R.; Peiris, J. S. M.; Bruzzone, R.; Nal, B. (15 November 2008). "The M, E, and N Structural Proteins of the Severe Acute Respiratory Syndrome Coronavirus Are Required for Efficient Assembly, Trafficking, and Release of Virus-Like Particles". Journal of Virology. 82 (22): 11318–11330. doi:10.1128/JVI.01052-08. PMC 2573274. PMID 18753196.
  15. ^ a b Alsaadi, Entedar A J; Jones, Ian M (April 2019). "Membrane binding proteins of coronaviruses". Future Virology. 14 (4): 275–286. doi:10.2217/fvl-2018-0144. PMC 7079996. PMID 32201500.
  16. ^ Nieto-Torres, Jose L.; DeDiego, Marta L.; Verdiá-Báguena, Carmina; Jimenez-Guardeño, Jose M.; Regla-Nava, Jose A.; Fernandez-Delgado, Raul; Castaño-Rodriguez, Carlos; Alcaraz, Antonio; Torres, Jaume; Aguilella, Vicente M.; Enjuanes, Luis (1 May 2014). "Severe Acute Respiratory Syndrome Coronavirus Envelope Protein Ion Channel Activity Promotes Virus Fitness and Pathogenesis". PLOS Pathogens. 10 (5): e1004077. doi:10.1371/journal.ppat.1004077. PMC 4006877. PMID 24788150.
  17. ^ a b Chai, Jin; Cai, Yuanheng; Pang, Changxu; Wang, Liguo; McSweeney, Sean; Shanklin, John; Liu, Qun (December 2021). "Structural basis for SARS-CoV-2 envelope protein recognition of human cell junction protein PALS1". Nature Communications. 12 (1): 3433. Bibcode:2021NatCo..12.3433C. doi:10.1038/s41467-021-23533-x. PMC 8187709. PMID 34103506.
  18. ^ Kuo, Lili; Hurst, Kelley R.; Masters, Paul S. (March 2007). "Exceptional Flexibility in the Sequence Requirements for Coronavirus Small Envelope Protein Function". Journal of Virology. 81 (5): 2249–2262. doi:10.1128/JVI.01577-06. PMC 1865940. PMID 17182690.
  19. ^ Rahman, M. Shaminur; Hoque, M. Nazmul; Islam, M. Rafiul; Islam, Israt; Mishu, Israt Dilruba; Rahaman, Md. Mizanur; Sultana, Munawar; Hossain, M. Anwar (March 2021). "Mutational insights into the envelope protein of SARS-CoV-2". Gene Reports. 22: 100997. doi:10.1016/j.genrep.2020.100997. PMC 7723457. PMID 33319124.
  20. ^ Bhattacharya, Shreya; Banerjee, Arundhati; Ray, Sujay (2021-03-01). "Development of new vaccine target against SARS-CoV2 using envelope (E) protein: An evolutionary, molecular modeling and docking based study". International Journal of Biological Macromolecules. 172: 74–81. doi:10.1016/j.ijbiomac.2020.12.192. PMC 7833863. PMID 33385461.
  21. ^ Chen, Jinni; Deng, Yao; Huang, Baoying; Han, Di; Wang, Wen; Huang, Mengjing; Zhai, Chengcheng; Zhao, Zhimin; Yang, Ren; Zhao, Ying; Wang, Wenling; Zhai, Desheng; Tan, Wenjie (2022-02-24). "DNA Vaccines Expressing the Envelope and Membrane Proteins Provide Partial Protection Against SARS-CoV-2 in Mice". Frontiers in Immunology. 13: 827605. doi:10.3389/fimmu.2022.827605. ISSN 1664-3224. PMC 8907653. PMID 35281016.

January 20, 2023
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The envelope E protein is the smallest and least well characterized of the four major structural proteins found in coronavirus virions 2 3 4 It is an integral membrane protein less than 110 amino acid residues long 2 in SARS CoV 2 the causative agent of Covid 19 the E protein is 75 residues long 5 Although it is not necessarily essential for viral replication absence of the E protein may produce abnormally assembled viral capsids or reduced replication 2 3 E is a multifunctional protein 6 and in addition to its role as a structural protein in the viral capsid it is thought to be involved in viral assembly likely functions as a viroporin and is involved in viral pathogenesis 2 5 Envelope proteinModel of the external structure of the SARS CoV 2 virion 1 Blue envelope Turquoise spike glycoprotein S Red envelope proteins E Green membrane proteins M Orange glycansIdentifiersSymbolCoV EPfamPF02723InterProIPR003873PROSITEPS51926Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summary Contents 1 Structure 1 1 Post translational modifications 2 Expression and localization 3 Function 3 1 Essentiality 3 2 Virions and viral assembly 3 3 Viroporin 3 4 Interactions with host proteins 4 Evolution and conservation 5 ReferencesStructure Edit Solid state NMR structure of the pentameric pore formed by the transmembrane helices of the SARS CoV 2 E protein which forms a viroporin permeable to cations 5 4 Rendered from PDB 7K3G The E protein consists of a short hydrophilic N terminal region a hydrophobic helical transmembrane domain and a somewhat hydrophilic C terminal region In SARS CoV and SARS CoV 2 the C terminal region contains a PDZ domain binding motif PBM 2 5 This feature appears to be conserved only in the alpha and beta coronavirus groups but not gamma 2 In the beta and gamma groups a conserved proline residue is found in the C terminal region likely involved in targeting the protein to the Golgi 2 The transmembrane helices of the E proteins of SARS CoV and SARS CoV 2 can oligomerize and have been shown in vitro to form pentameric structures with central pores that serve as cation selective ion channels 5 Both viruses E protein pentamers have been structurally characterized by nuclear magnetic resonance spectroscopy 5 7 The membrane topology of the E protein has been studied in a number of coronaviruses with inconsistent results the protein s orientation in the membrane may be variable 3 The balance of evidence suggests the most common orientation has the C terminus oriented toward the cytoplasm 8 Studies of SARS CoV 2 E protein are consistent with this orientation 5 9 Post translational modifications Edit In some but not all coronaviruses the E protein is post translationally modified by palmitoylation on conserved cysteine residues 2 8 In the SARS CoV E protein one glycosylation site has been observed which may influence membrane topology 8 however the functional significance of E glycosylation is unclear 2 Ubiquitination of SARS CoV E has also been described though its functional significance is also not known 2 Expression and localization EditGenomic information Genomic organisation of isolate Wuhan Hu 1 the earliest sequenced sample of SARS CoV 2 indicating the location of the E geneNCBI genome ID86693Genome size29 903 basesYear of completion2020Genome browser UCSC The E protein is expressed at high abundance in infected cells However only a small amount of the total E protein produced is found in assembled virions 2 4 E protein is localized to the endoplasmic reticulum Golgi apparatus and endoplasmic reticulum Golgi intermediate compartment ERGIC the intracellular compartment that gives rise to the coronavirus viral envelope 2 5 Function EditEssentiality Edit Studies in different coronaviruses have reached different conclusions about whether E is essential to viral replication In some coronaviruses including MERS CoV E has been reported to be essential 10 In others including mouse coronavirus 11 and SARS CoV E is not essential though its absence reduces viral titer 12 in some cases by introducing propagation defects or causing abnormal capsid morphology 2 Virions and viral assembly Edit Illustration of a coronavirus virion in the respiratory mucosa showing the positions of the four structural proteins and components of the extracellular environment 13 The E protein is found in assembled virions where it forms protein protein interactions with the coronavirus membrane protein M the most abundant of the four structural proteins contained in the viral capsid 2 4 The interaction between E and M occurs through their respective C termini on the cytoplasmic side of the membrane 2 In most coronaviruses E and M are sufficient to form virus like particles 2 4 though SARS CoV has been reported to depend on N as well 14 There is good evidence that E is involved in inducing membrane curvature to create the typical spherical coronavirus virion 2 15 It is likely that E is involved in viral budding or scission although its role in this process has not been well characterized 2 4 15 Viroporin Edit In its pentameric state E forms cation selective ion channels and likely functions as a viroporin 5 This may disrupt ion homeostasis alter membrane permeability and modulate pH in the host cell which may facilitate viral release 2 4 The E protein s role as a viroporin appears to be involved in pathogenesis and may be related to activation of the inflammasome 3 16 In SARS CoV mutations that disrupt E s ion channel function result in attenuated pathogenesis in animal models despite little effect on viral growth 10 Interactions with host proteins Edit Cryo electron microscopy structure of the interaction between the SARS CoV 2 E protein PDZ binding motif magenta and a construct containing the PDZ blue SH3 yellow and guanylate kinase like GK green domains from a host cell protein human PALS1 17 Protein protein interactions between E and proteins in the host cell are best described in SARS CoV and occur via the C terminal PDZ domain binding motif The SARS CoV E protein has been reported to interact with five host cell proteins Bcl xL PALS1 syntenin sodium potassium Na K ATPase a 1 subunit and stomatin 2 The interaction with PALS1 may be related to pathogenesis via the resulting disruption in tight junctions 3 10 This interaction has also been identified in SARS CoV 2 17 Evolution and conservation EditThe sequence of the E protein is not well conserved across coronavirus genera with sequence identities reaching under 30 12 In laboratory experiments on mouse hepatitis virus substitution of E proteins from different coronaviruses even from different groups could produce viable viruses suggesting that significant sequence diversity can be tolerated in functional E proteins 18 The SARS CoV 2 E protein is very similar to that of SARS CoV with three substitutions and one deletion 4 A study of SARS CoV 2 sequences suggests that the E protein is evolving relatively slowly compared to other structural proteins 19 The conserved nature of the envelope protein among SARS CoV and SARS CoV 2 variants has led it to be researched as a potential target for universal coronavirus vaccine development 20 21 References Edit Solodovnikov Alexey Arkhipova Valeria 2021 07 29 Dostoverno krasivo kak my sdelali 3D model SARS CoV 2 Truly beautiful how we made the SARS CoV 2 3D model in Russian N 1 Archived from the original on 2021 07 30 Retrieved 30 July 2021 a b c d e f g h i j k l m n o p q r s t Schoeman Dewald Fielding Burtram C December 2019 Coronavirus envelope protein current knowledge Virology Journal 16 1 69 doi 10 1186 s12985 019 1182 0 PMC 6537279 PMID 31133031 a b c d e Schoeman Dewald Fielding Burtram C 2020 09 03 Is There a Link Between the Pathogenic Human Coronavirus Envelope Protein and Immunopathology A Review of the Literature Frontiers in Microbiology 11 2086 doi 10 3389 fmicb 2020 02086 PMC 7496634 PMID 33013759 a b c d e f g h Cao Yipeng Yang Rui Lee Imshik Zhang Wenwen Sun Jiana Wang Wei Meng Xiangfei June 2021 Characterization of the SARS CoV 2 E Protein Sequence Structure Viroporin and Inhibitors Protein Science 30 6 1114 1130 doi 10 1002 pro 4075 ISSN 0961 8368 PMC 8138525 PMID 33813796 a b c d e f g h i Mandala Venkata S McKay Matthew J Shcherbakov Alexander A Dregni Aurelio J Kolocouris Antonios Hong Mei December 2020 Structure and drug binding of the SARS CoV 2 envelope protein transmembrane domain in lipid bilayers Nature Structural amp Molecular Biology 27 12 1202 1208 doi 10 1038 s41594 020 00536 8 PMC 7718435 PMID 33177698 Liu D X Yuan Q Liao Y August 2007 Coronavirus envelope protein A small membrane protein with multiple functions Cellular and Molecular Life Sciences 64 16 2043 2048 doi 10 1007 s00018 007 7103 1 PMC 7079843 PMID 17530462 Surya Wahyu Li Yan Torres Jaume June 2018 Structural model of the SARS coronavirus E channel in LMPG micelles Biochimica et Biophysica Acta BBA Biomembranes 1860 6 1309 1317 doi 10 1016 j bbamem 2018 02 017 PMC 7094280 PMID 29474890 a b c Fung To Sing Liu Ding Xiang June 2018 Post translational modifications of coronavirus proteins roles and function Future Virology 13 6 405 430 doi 10 2217 fvl 2018 0008 PMC 7080180 PMID 32201497 Duart Gerard Garcia Murria Mª Jesus Grau Brayan Acosta Caceres Jose M Martinez Gil Luis Mingarro Ismael September 2020 SARS CoV 2 envelope protein topology in eukaryotic membranes Open Biology 10 9 200209 doi 10 1098 rsob 200209 PMC 7536074 PMID 32898469 a b c DeDiego Marta L Nieto Torres Jose L Jimenez Guardeno Jose M Regla Nava Jose A Castano Rodriguez Carlos Fernandez Delgado Raul Usera Fernando Enjuanes Luis December 2014 Coronavirus virulence genes with main focus on SARS CoV envelope gene Virus Research 194 124 137 doi 10 1016 j virusres 2014 07 024 PMC 4261026 PMID 25093995 Kuo Lili Masters Paul S 2003 04 15 The Small Envelope Protein E Is Not Essential for Murine Coronavirus Replication Journal of Virology 77 8 4597 4608 doi 10 1128 JVI 77 8 4597 4608 2003 PMC 152126 PMID 12663766 a b Ruch Travis R Machamer Carolyn E 2012 03 08 The Coronavirus E Protein Assembly and Beyond Viruses 4 3 363 382 doi 10 3390 v4030363 PMC 3347032 PMID 22590676 Goodsell David S Voigt Maria Zardecki Christine Burley Stephen K 6 August 2020 Integrative illustration for coronavirus outreach PLOS Biology 18 8 e3000815 doi 10 1371 journal pbio 3000815 PMC 7433897 PMID 32760062 Siu Y L Teoh K T Lo J Chan C M Kien F Escriou N Tsao S W Nicholls J M Altmeyer R Peiris J S M Bruzzone R Nal B 15 November 2008 The M E and N Structural Proteins of the Severe Acute Respiratory Syndrome Coronavirus Are Required for Efficient Assembly Trafficking and Release of Virus Like Particles Journal of Virology 82 22 11318 11330 doi 10 1128 JVI 01052 08 PMC 2573274 PMID 18753196 a b Alsaadi Entedar A J Jones Ian M April 2019 Membrane binding proteins of coronaviruses Future Virology 14 4 275 286 doi 10 2217 fvl 2018 0144 PMC 7079996 PMID 32201500 Nieto Torres Jose L DeDiego Marta L Verdia Baguena Carmina Jimenez Guardeno Jose M Regla Nava Jose A Fernandez Delgado Raul Castano Rodriguez Carlos Alcaraz Antonio Torres Jaume Aguilella Vicente M Enjuanes Luis 1 May 2014 Severe Acute Respiratory Syndrome Coronavirus Envelope Protein Ion Channel Activity Promotes Virus Fitness and Pathogenesis PLOS Pathogens 10 5 e1004077 doi 10 1371 journal ppat 1004077 PMC 4006877 PMID 24788150 a b Chai Jin Cai Yuanheng Pang Changxu Wang Liguo McSweeney Sean Shanklin John Liu Qun December 2021 Structural basis for SARS CoV 2 envelope protein recognition of human cell junction protein PALS1 Nature Communications 12 1 3433 Bibcode 2021NatCo 12 3433C doi 10 1038 s41467 021 23533 x PMC 8187709 PMID 34103506 Kuo Lili Hurst Kelley R Masters Paul S March 2007 Exceptional Flexibility in the Sequence Requirements for Coronavirus Small Envelope Protein Function Journal of Virology 81 5 2249 2262 doi 10 1128 JVI 01577 06 PMC 1865940 PMID 17182690 Rahman M Shaminur Hoque M Nazmul Islam M Rafiul Islam Israt Mishu Israt Dilruba Rahaman Md Mizanur Sultana Munawar Hossain M Anwar March 2021 Mutational insights into the envelope protein of SARS CoV 2 Gene Reports 22 100997 doi 10 1016 j genrep 2020 100997 PMC 7723457 PMID 33319124 Bhattacharya Shreya Banerjee Arundhati Ray Sujay 2021 03 01 Development of new vaccine target against SARS CoV2 using envelope E protein An evolutionary molecular modeling and docking based study International Journal of Biological Macromolecules 172 74 81 doi 10 1016 j ijbiomac 2020 12 192 PMC 7833863 PMID 33385461 Chen Jinni Deng Yao Huang Baoying Han Di Wang Wen Huang Mengjing Zhai Chengcheng Zhao Zhimin Yang Ren Zhao Ying Wang Wenling Zhai Desheng Tan Wenjie 2022 02 24 DNA Vaccines Expressing the Envelope and Membrane Proteins Provide Partial Protection Against SARS CoV 2 in Mice Frontiers in Immunology 13 827605 doi 10 3389 fimmu 2022 827605 ISSN 1664 3224 PMC 8907653 PMID 35281016 Retrieved from https en wikipedia org w index php title Coronavirus envelope protein amp oldid 1115726955, wikipedia, wiki, book, books, library,

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