M protein oligomerization

Stable Identifier
Reaction [binding]
Homo sapiens
Related Species
Human SARS coronavirus
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M protein is the most abundant component of the mature virionm and contributes to the shape of the virus. It consists of three transmembrane domains with an N-terminus outside the virus and an internal C-terminus (N-exo, C-endo conformation). Homotypic interactions between M proteins contribute to the initial formation of a nascent virus by forming a lattice, consistent with what is seen in other coronavirus systems (Tseng et al, 2010; de Hann et al, 1998; de Haan et al, 2000; Locker et al, 1995). Multiple segments of M are required for oligomerization (Tseng et al, 2010; de Hann et al, 1998; de Haan et al, 2000; reviewed in Masters, 2006). Both glycosylated and non-glycosylated forms of M are incorporated into the virion, and the significance of the N-linked glycosylation is not clear (Voss et al, 2006; Voss et al, 2009).
Despite its importance, expression of M alone is not sufficient to drive formation of a mature virus (reviewed in Masters, 2006). Protein-protein interactions between M and S, N and E, among other components, are required for assembly of a mature virus and for membrane curvature. Many studies have examined the minimal system required for release of viral like particles (VLPs) with sometimes contradictory results, but interactions between M, N and E are sufficient to promote release of significant numbers of VLPs (Ho et al, 2004; Huang et al, 2004; Mortola and Roy, 2004; Hsieh et al, 2005; Siu et al, 2008; Hatakeyama et al, 2008; Tseng et al, 2013; reviewed in Masters, 2006)

Literature References
PubMed ID Title Journal Year
23700447 Identifying SARS-CoV membrane protein amino acid residues linked to virus-like particle assembly

Chang, CH, Tseng, YT, Wang, SM, Huang, KJ, Wang, CT

PLoS ONE 2013
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
20154085 Self-assembly of severe acute respiratory syndrome coronavirus membrane protein

Tseng, YT, Wang, SM, Chiang, CC, Huang, KJ, Lee, AI, Wang, CT

J. Biol. Chem. 2010
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
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
15474033 Efficient assembly and release of SARS coronavirus-like particles by a heterologous expression system

Mortola, E, Roy, P

FEBS Lett. 2004
9658133 Coronavirus particle assembly: primary structure requirements of the membrane protein

Kuo, L, de Haan, CA, Rottier, PJ, Masters, PS, Vennema, H

J. Virol. 1998
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
19534833 Studies on membrane topology, N-glycosylation and functionality of SARS-CoV membrane protein

Voss, D, Drosten, C, Lanzavecchia, A, Pfefferle, S, Stevermann, L, Becker, S, Traggiai, E

Virol. J. 2009
16877062 The molecular biology of coronaviruses

Masters, PS

Adv. Virus Res. 2006
10799570 Assembly of the coronavirus envelope: homotypic interactions between the M proteins

de Haan, CA, Rottier, PJ, Vennema, H

J. Virol. 2000
16442106 Characterization of severe acute respiratory syndrome coronavirus membrane protein

Eickmann, M, Voss, D, Kern, A, Lanzavecchia, A, Becker, S, Traggiai, E, Stadler, K

FEBS Lett. 2006
7721788 Oligomerization of a trans-Golgi/trans-Golgi network retained protein occurs in the Golgi complex and may be part of its retention

Opstelten, DJ, Locker, JK, Rottier, PJ, Ericsson, M, Horzinek, MC

J. Biol. Chem. 1995
Orthologous Events
Name Identifier Synonyms
severe acute respiratory syndrome DOID:2945 SARS-CoV infection, SARS
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