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VP40

From Wikipedia, the free encyclopedia
Virus matrix protein
For the Heckler & Koch semi-automatic handgun, seeHK VP40.
Protein family
VP40
VP40 matrix protein hexamer, Ebola virus
Identifiers
SymbolVP40
PfamPF07447
InterProIPR008986
SCOP21h2c /SCOPe /SUPFAM
Available protein structures:
Pfam  structures /ECOD  
PDBRCSB PDB;PDBe;PDBj
PDBsumstructure summary

In molecular biology,VP40 is the name of aviral matrix protein. Most commonly, it is found in theEbola virus (EBOV),[1] a type of non-segmented, negative-strandRNAvirus. Ebola virus causes a severe and often fatalhaemorrhagic fever inhumans, known asEbola virus disease. The virus matrixprotein VP40 is a majorstructural protein that plays a central role in virus assembly andbudding at theplasma membrane of infectedcells. VP40proteins work by associating withcellular membranes,interacting with thecytoplasmic tails of glycoproteins andbinding to theribonucleoproteincomplex.[citation needed]

Structure

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The VP40monomer consists of twoprotein domains, theN-terminal oligomerization domain and theC-terminal membrane-binding domain, connected by a flexible linker. Both the N- and C-terminaldomainsfold intobeta sandwichstructures of similar topology.[2] Within the N-terminal domain are two overlapping L-domains with thesequences PTAP and PPEY atresidues 7 to 13, which are required for efficient budding.[3] L-domains are thought to mediate their function in budding through their interaction with specific host cellular proteins, such asTSG101 and vps-4.[4]

Function

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Different structures VP40 assumes in its functional roles

VP40 coordinates numerous functions in the viral life cycle of theEbola virus. These include: regulation of viraltranscription,morphogenesis, packaging and budding of mature virions.[5]

VP40 goes through intermediate states of assembly (e.g. octamers). It has been noted that proteins encoded by EBOV (VP30, VP35, and VP40) act independently as suppressors ofRNA silencing, indicating that the virus actively resists cellular RNAi during replication.[5]

Significance of VP40

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VP40 position in the Ebola virus genome

Study of the matrix protein VP40 is important due to the highmortality rate of the Ebola virus, which is listed as aWHO Risk Group 4 Pathogen, anHHSSelect Agent, anNIH/NIAID Category A Priority Pathogen, aCDC Category A Bioterrorism Agent, and a Biological Agent for Export Control by theAustralia Group.[5]

Expression of the matrix protein VP40 is sufficient to generatevirus-like particles (no viral genetic material) in amammalian host that are remarkably indistinguishable from live virus, from a morphological standpoint.[5]

West African Ebola virus outbreak

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During and after the 2014-2016West African Ebola virus epidemic treatment options were sought; among them were the VP40 matrix protein as a target for possible research that may (or may not) lead to a therapeutic option.[6][7]

References

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  1. ^Dessen, Andréa; Volchkov, Viktor; Dolnik, Olga; Klenk, Hans-Dieter; Weissenhorn, Winfried (2000-08-15)."Crystal structure of the matrix protein VP40 from Ebola virus".The EMBO Journal.19 (16):4228–4236.doi:10.1093/emboj/19.16.4228.ISSN 0261-4189.PMC 302032.PMID 10944105.
  2. ^Dessen A, Volchkov V, Dolnik O, Klenk HD, Weissenhorn W (August 2000)."Crystal structure of the matrix protein VP40 from Ebola virus".EMBO J.19 (16):4228–36.doi:10.1093/emboj/19.16.4228.PMC 302032.PMID 10944105.
  3. ^Timmins J, Schoehn G, Ricard-Blum S, Scianimanico S, Vernet T, Ruigrok RW, Weissenhorn W (February 2003). "Ebola virus matrix protein VP40 interaction with human cellular factors Tsg101 and Nedd4".J. Mol. Biol.326 (2):493–502.doi:10.1016/S0022-2836(02)01406-7.PMID 12559917.
  4. ^Licata JM, Simpson-Holley M, Wright NT, Han Z, Paragas J, Harty RN (February 2003)."Overlapping motifs (PTAP and PPEY) within the Ebola virus VP40 protein function independently as late budding domains: involvement of host proteins TSG101 and VPS-4".J. Virol.77 (3):1812–9.doi:10.1128/jvi.77.3.1812-1819.2003.PMC 140960.PMID 12525615.
  5. ^abcdSilva LP, Vanzile M, Bavari S, Aman JM, Schriemer DC (2012)."Assembly of Ebola Virus Matrix Protein VP40 Is Regulated by Latch-Like Properties of N and C Terminal Tails".PLOS ONE.7 (7): e39978.Bibcode:2012PLoSO...739978S.doi:10.1371/journal.pone.0039978.PMC 3390324.PMID 22792204.
  6. ^Madara, Jonathan J; Han, Ziying; Ruthel, Gordon; Freedman, Bruce D; Harty, Ronald N (2017-02-05)."The multifunctional Ebola virus VP40 matrix protein is a promising therapeutic target".Future Virology.10 (5):537–546.doi:10.2217/fvl.15.6.ISSN 1746-0794.PMC 4480923.PMID 26120351.
  7. ^Balmith, Marissa; Soliman, Mahmoud E. S. (2017-02-01). "VP40 of the Ebola Virus as a Target for EboV Therapy: Comprehensive Conformational and Inhibitor Binding Landscape from Accelerated Molecular Dynamics".Cell Biochemistry and Biophysics.75 (1):65–78.doi:10.1007/s12013-017-0783-8.ISSN 1559-0283.PMID 28144904.S2CID 26535324.subscription needed
This article incorporates text from the public domainPfam andInterPro:IPR008986
DNA
linear ds-DNA
(Duplodnaviria,
Varidnaviria)
Herpes simplex
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capsid:
VNPs:
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Adenoviridae
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(Duplodnaviria,
Varidnaviria?)
Epstein–Barr
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Baculoviridae
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Polyomaviridae
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(non-enveloped circular ds-DNA)
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