Coronavirus membrane protein

Source: Wikipedia, the free encyclopedia.
Membrane protein
virion.[1]
● Blue: envelope
● Turquoise: spike glycoprotein (S)
● Red: envelope proteins (E)
● Green: membrane proteins (M)
● Orange: glycans
Identifiers
SymbolCoV_M
PfamPF01635
InterProIPR002574
PROSITEPS51927
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

The membrane (M) protein (previously called E1, sometimes also matrix protein

protein-protein interactions with other M protein molecules as well as with the other three structural proteins, the envelope (E), spike (S), and nucleocapsid (N) proteins.[4][6][7][8]

Structure

The M protein is a

amphipathic region near the C-terminal end of the third transmembrane segment.[8][9]

M functions as a

protein-protein interactions with other structural proteins.[5] M protein of SARS-CoV-2 is homologous to the prokaryotic sugar transport protein SemiSWEET.[11]

Post-translational modifications

M is a

SARS-CoV, a betacoronavirus, the M protein has one N-glycosylation site.[8][6] Glycosylation state does not appear to have a measurable effect on viral growth.[6][9][12] No other post-translational modifications have been described for the M protein.[4]

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 M gene
NCBI genome ID86693
Genome size29,903 bases
Year of completion2020
Genome browser (UCSC)

The

MERS-CoV M protein found C-terminal sequence signals associated with trafficking to the Golgi.[14]

Function

respiratory mucosa, showing the positions of the four structural proteins and components of the extracellular environment.[15]

The M protein is the most abundant protein in coronavirus

virions.[8][5][4] It is essential for viral replication.[4]

Viral assembly

The primary function of the M protein is organizing assembly of new virions.[4] It is involved in establishing viral shape and morphology. Individual M molecules interact with each other to form the viral envelope[7][9][8] and may be able to exclude host cell proteins from the viral membrane.[5] Studies of the SARS-CoV M protein suggest that M-M interactions involve both the N- and C-termini.[6] Coronaviruses are moderately pleomorphic and conformational variations of M appear to be associated with virion size.[5]

M forms

viral budding.[7] M also appears to have functional roles in the later stages of viral maturation, secretion, and budding.[4]

Incorporation of the spike protein (S) - which is required for assembly of infectious virions - is reported to occur though M interactions and may depend on specific conformations of M.[5][13] The conserved amphipathic region C-terminal to the third transmembrane segment is important for spike interactions.[13] Interactions with M appear to be required for correct subcellular localization of S at the viral budding site.[12] M interacts directly with the nucleocapsid (N) protein without requiring the presence of RNA.[6] This interaction appears to occur primarily through both proteins' C-termini.[4]

Interactions with the immune system

SARS-CoV (yellow, shown as surface). From PDB: 3I6G​.[16]

The M protein in

SARS-CoV, and SARS-CoV-2 has been described as an antagonist of interferon response.[4][17]

The M protein is

severe acute respiratory syndrome (SARS).[18]

Other recent research has identified that SAS-COV-2 membrane protein when treated on human PBMC's causes a significant increase in pro inflammatory mediators such as TNF and IL-6.[19] The effects of exogenous SARS-COV-2 membrane protein challenge in mice was also studied. In these studies, exogenous membrane protein treated intra nasally caused a significant increase in pulmonary inflammation in mice leading to histological changes within the lungs.[20]

Host cell entry

It has been reported that

heparan sulfate proteoglycans exposed on the cell surface.[21]

Evolution and conservation

A study of SARS-CoV-2 sequences collected during the

non-structural proteins in the coronavirus genome are most subject to evolutionary constraints.[23]

References

  1. ^ Solodovnikov, Alexey; Arkhipova, Valeria (2021-07-29). "Достоверно красиво: как мы сделали 3D-модель 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.
  2. PMID 15626342
    .
  3. ^ Thomas S. The Structure of the Membrane Protein of SARS-CoV-2 Resembles the Sugar Transporter SemiSWEET. Pathog Immun. 2020 Oct 19;5(1):342-363.
  4. ^
    PMID 33525632
    .
  5. ^
    PMID 21130884
    .
  6. ^
    PMID 20154085
    .
  7. ^
    PMID 31133031
    .
  8. ^
    PMID 16877062
    .
  9. ^
    PMID 32201500
    .
  10. PMID 33813796
    .
  11. ^ Thomas S. The Structure of the Membrane Protein of SARS-CoV-2 Resembles the Sugar Transporter SemiSWEET. Pathog Immun. 2020 Oct 19;5(1):342-363
  12. ^
    PMID 19534833
    .
  13. ^
    PMID 25855243
    .
  14. PMID 31399512
    .
  15. PMID 32760062
    .
  16. ^
    PMID 20831383
    .
  17. PMID 33372174
    .
  18. PMID 15448374
    .
  19. ^ Haystead, T., Lee, E., Cho, K., Gullickson, G., Hughes, P., Krafsur, G., ... & Scarneo, S. (2023). Investigation of SARS-CoV-2 individual proteins reveals the in vitro and in vivo immunogenicity of membrane protein. Scientific Reports, 13(1), 22873.
  20. ^ Haystead, T., Lee, E., Cho, K., Gullickson, G., Hughes, P., Krafsur, G., ... & Scarneo, S. (2023). Investigation of SARS-CoV-2 individual proteins reveals the in vitro and in vivo immunogenicity of membrane protein. Scientific Reports, 13(1), 22873.
  21. PMID 31315999
    .
  22. PMID 33896413
    .
  23. PMID 32238584
    .
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