E and N are recruited to the M lattice

Stable Identifier
R-HSA-9684238
Type
Reaction [binding]
Species
Homo sapiens
Related Species
Human SARS coronavirus
Compartment
endoplasmic reticulum-Golgi intermediate compartment membrane
ReviewStatus
5/5
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E and N are recruited to the M lattice
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Formation of an M lattice nucleates recruitment of other structural proteins including N, E and S (reviewed in Masters, 2006; Fung and Liu, 2019; Ujike and Taguchi, 2015). Expression of M and N or M and E have been shown to be sufficient to support release of viral like particles (VLPs), with co-expression of all three promoting release of significant numbers of VLPs (Huang et al, 2004; Ho et al, 2004; Hsieh et al, 2005; Mortola and Roy, 2004; Siu et al, 2008). Neither the S protein nor the genomic RNA are required for release of these otherwise morphologically normal particles, but both are incorporated if co-expressed (Siu et al, 2008).
E protein is a small, integral membrane protein that is present in low amounts in the mature virion. It forms homo-oligomers and may exist as a homopentamer (Torres et al, 2005). E is palmitoylated and N-glycosylated, although the significance of these modifications is not clear (Liao et al, 2006; Yuan et al, 2006). E is recruited to the M lattice through interactions between the transmembrane domains of both proteins, and plays multiple roles in virion assembly and host interactions, including membrane budding, induction of apoptosis and membrane permeability (Hsieh et al, 2008; Chen et al, 2009; reviewed in Schoeman and Fielding, 2019; Liu et al, 2016).
The ribonucleoprotein complex is recruited to the assembling virion through interactions with the M C-terminal tail, and appears to be independent of viral RNA (Hsieh et al, 2008; Hatakeyama et al, 2008; He et al, 2004; Luo et al, 2006; reviewed in Ujike and Taguchi, 2015).
Literature References
PubMed ID Title Journal Year
16254320 Assembly of severe acute respiratory syndrome coronavirus RNA packaging signal into virus-like particles is nucleocapsid dependent

Hsieh, PK, Chang, CK, Lee, TT, Hsiao, CW, Huang, CC, Chen, IY, Kou, YH, Chang, MF, Huang, TH, Chang, SC

J. Virol. 2005
15507643 Generation of synthetic severe acute respiratory syndrome coronavirus pseudoparticles: implications for assembly and vaccine production

Kong, WP, Huang, Y, Nabel, GJ, Yang, ZY

J. Virol. 2004
17530462 Coronavirus envelope protein: a small membrane protein with multiple functions

Liao, Y, Liu, DX, Yuan, Q

Cell. Mol. Life Sci. 2007
15147946 Assembly of human severe acute respiratory syndrome coronavirus-like particles

Lee, SP, Chao, YC, Ho, Y, Lin, PH, Liu, CY

Biochem. Biophys. Res. Commun. 2004
31133031 Coronavirus envelope protein: current knowledge

Schoeman, D, Fielding, BC

Virol. J. 2019
25855243 Incorporation of spike and membrane glycoproteins into coronavirus virions

Ujike, M, Taguchi, F

Viruses 2015
15351485 Characterization of protein-protein interactions between the nucleocapsid protein and membrane protein of the SARS coronavirus

Li, Y, Tyler, S, Strocher, U, Booth, TF, Theriault, S, Bastien, N, Baker, L, He, R, Plummer, FA, Cao, J, Feldmann, H, Cutts, T, Ballantine, M, Li, X, Dobie, F, Leeson, A, Andonov, A

Virus Res. 2004
16684538 Biochemical evidence for the presence of mixed membrane topologies of the severe acute respiratory syndrome coronavirus envelope protein expressed in mammalian cells

Liu, DX, Liao, Y, Tam, JP, Yuan, Q, Torres, J

FEBS Lett. 2006
16507314 Biochemical and functional characterization of the membrane association and membrane permeabilizing activity of the severe acute respiratory syndrome coronavirus envelope protein

Liu, DX, Liao, Y, Tam, JP, Yuan, Q, Torres, J

Virology 2006
15474033 Efficient assembly and release of SARS coronavirus-like particles by a heterologous expression system

Mortola, E, Roy, P

FEBS Lett. 2004
16343974 Severe acute respiratory syndrome coronavirus membrane protein interacts with nucleocapsid protein mostly through their carboxyl termini by electrostatic attraction

Shen, X, Shen, C, Luo, H, Jiang, H, Wu, D, Chen, K

Int. J. Biochem. Cell Biol. 2006
15713601 The transmembrane oligomers of coronavirus protein E

Parthasarathy, K, Liu, DX, Wang, J, Torres, J

Biophys. J. 2005
18703211 Dissection and identification of regions required to form pseudoparticles by the interaction between the nucleocapsid (N) and membrane (M) proteins of SARS coronavirus

Kanai, T, Itoh, K, Shichijo, S, Miyoshi-Akiyama, T, Sasazuki, T, Kirikae, T, Fukushi, M, Hatakeyama, S, Komatsu, N, Ishida, I, Matsuoka, Y, Ueshiba, H

Virology 2008
18753196 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

Nicholls, JM, Nal, B, Altmeyer, R, Bruzzone, R, Teoh, KT, Kien, F, Chan, CM, Escriou, N, Tsao, SW, Peiris, JS, Siu, YL, Lo, J

J. Virol. 2008
18792806 Interactions between M protein and other structural proteins of severe, acute respiratory syndrome-associated coronavirus

Chen, SC, Li, HC, Lo, SY, Hsieh, YC

J. Biomed. Sci. 2008
16877062 The molecular biology of coronaviruses

Masters, PS

Adv. Virus Res. 2006
31226023 Human Coronavirus: Host-Pathogen Interaction

Fung, TS, Liu, DX

Annu. Rev. Microbiol. 2019
19322648 Expression and membrane integration of SARS-CoV E protein and its interaction with M protein

Chen, SC, Li, HC, Ma, HC, Lo, SY

Virus Genes 2009
Participants
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Output
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Orthologous Events
E and N are recruited to the M lattice (Homo sapiens)
Disease
Name Identifier Synonyms
severe acute respiratory syndrome DOID:2945 SARS-CoV infection, SARS
Authored
Rothfels, K  (2020-04-22)
Reviewed
Acencio, ML  (2020-05-27)
Mazein, A  (2020-05-27)
Created
Rothfels, K  (2020-04-21)
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