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Gene Review

VP40  -  matrix protein

Reston ebolavirus

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Disease relevance of VP40

  • These data demonstrate that the VP40 protein of Ebola virus possesses a PY motif that is functionally similar to those described previously for Gag and M proteins of specific retroviruses and rhabdoviruses, respectively [1].
  • Refolding experiments with a nucleic acid free N-terminal domain preparation reveal a mostly dimeric form of VP40, which is transformed into an SDS resistant octamer upon incubation with E. coli nucleic acids [2].
  • Coexpression of the Ebola virus glycoprotein (GP) and matrix protein (VP40) in mammalian cells results in spontaneous production and release of virus-like particles (VLPs) that resemble the distinctively filamentous infectious virions [3].
  • Recombinant baculoviruses (rBV) expressing Ebola virus VP40 (rBV-VP40) or GP (rBV-GP) proteins were generated [4].

High impact information on VP40

  • In addition, we demonstrate that membrane association of wild-type VP40 also induces the conformational switch from monomeric to hexameric molecules that may form the building blocks for initiation of virus assembly and budding [5].
  • The matrix protein VP40 from Ebola virus is targeted to the plasma membrane, where it is thought to induce assembly and budding of virions through its association with the lipid bilayer [5].
  • By mutagenesis, we identify several critical C-terminal sequences that regulate oligomerization at the plasma membrane, association with detergent-resistant membranes, and vesicular release of VP40, directly linking these phenomena [6].
  • Single point mutations that disrupted the PY motif of VP40 abolished the PY/WW-domain interactions [1].
  • The presence of VP40-associated microtubules in cells continuously treated with nocodazole suggested that VP40 promotes tubulin polymerization [7].

Biological context of VP40


Anatomical context of VP40

  • While wild-type VP40 was present in small patches predominantly at the plasma membrane, the octamer-negative mutants were found in larger aggregates at the periphery of the cell and in the perinuclear region [10].
  • Nine stable hybridoma cell lines were obtained producing specific mAbs directed against the viral structural protein VP40 [11].
  • When transfected into mammalian cells, a fraction of VP40 colocalized with microtubule bundles and VP40 coimmunoprecipitated with tubulin [7].
  • Here we show that virus-like particles (VLPs) consisting of the Ebola virus matrix protein VP40 and GP(1,2) were able to activate endothelial cells and induce a decrease in barrier function as determined by impedance spectroscopy and hydraulic conductivity measurements [12].

Associations of VP40 with chemical compounds

  • Triton X-114 phase-partitioning analysis suggested that VP40 possesses only minor features of an integral membrane protein [13].
  • Ebola virus budding is mediated by two proline-rich motifs, PPxY and PTAP, within the viral matrix protein VP40 [14].
  • Previously, we showed that expression of the homologous glycoprotein (GP) and matrix protein VP40 from a single filovirus, either EBOV or MARV, resulted in formation of wild-type virus-like particles (VLPs) in mammalian cells [15].

Regulatory relationships of VP40

  • Overall, these findings indicate that major changes in morphology of VP40 VLPs were likely not responsible for enhanced budding of VP40 VLPs in the presence of GP, NP and/or VP35 [16].

Other interactions of VP40

  • Effect of Ebola virus proteins GP, NP and VP35 on VP40 VLP morphology [16].

Analytical, diagnostic and therapeutic context of VP40

  • To explore the possibility that VLP structure was altered by co-expression of EBOV proteins leading to the observed enhancement of VP40 VLP budding, we performed density gradient analysis as well as electron microscopy studies [16].
  • This assay detects both Ebola virus and EBOV-like particles (VLPs) directly from cell-culture supernatants with the VP40 matrix protein serving as antigen [17].
  • Subsequently, an antigen capture enzyme-linked immunosorbent assay was established, which detects VP40 of all known species of EBOV [11].


  1. A PPxY motif within the VP40 protein of Ebola virus interacts physically and functionally with a ubiquitin ligase: implications for filovirus budding. Harty, R.N., Brown, M.E., Wang, G., Huibregtse, J., Hayes, F.P. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  2. Oligomerization and polymerization of the filovirus matrix protein VP40. Timmins, J., Schoehn, G., Kohlhaas, C., Klenk, H.D., Ruigrok, R.W., Weissenhorn, W. Virology (2003) [Pubmed]
  3. Ebola virus-like particles protect from lethal Ebola virus infection. Warfield, K.L., Bosio, C.M., Welcher, B.C., Deal, E.M., Mohamadzadeh, M., Schmaljohn, A., Aman, M.J., Bavari, S. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  4. Ebola virus-like particles produced in insect cells exhibit dendritic cell stimulating activity and induce neutralizing antibodies. Ye, L., Lin, J., Sun, Y., Bennouna, S., Lo, M., Wu, Q., Bu, Z., Pulendran, B., Compans, R.W., Yang, C. Virology (2006) [Pubmed]
  5. Membrane association induces a conformational change in the Ebola virus matrix protein. Scianimanico, S., Schoehn, G., Timmins, J., Ruigrok, R.H., Klenk, H.D., Weissenhorn, W. EMBO J. (2000) [Pubmed]
  6. In vivo oligomerization and raft localization of Ebola virus protein VP40 during vesicular budding. Panchal, R.G., Ruthel, G., Kenny, T.A., Kallstrom, G.H., Lane, D., Badie, S.S., Li, L., Bavari, S., Aman, M.J. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  7. Association of ebola virus matrix protein VP40 with microtubules. Ruthel, G., Demmin, G.L., Kallstrom, G., Javid, M.P., Badie, S.S., Will, A.B., Nelle, T., Schokman, R., Nguyen, T.L., Carra, J.H., Bavari, S., Aman, M.J. J. Virol. (2005) [Pubmed]
  8. An all-atom model of the pore-like structure of hexameric VP40 from Ebola: structural insights into the monomer-hexamer transition. Nguyen, T.L., Schoehn, G., Weissenhorn, W., Hermone, A.R., Burnett, J.C., Panchal, R.G., McGrath, C., Zaharevitz, D.W., Aman, M.J., Gussio, R., Bavari, S. J. Struct. Biol. (2005) [Pubmed]
  9. Differentiation of filoviruses by electron microscopy. Geisbert, T.W., Jahrling, P.B. Virus Res. (1995) [Pubmed]
  10. VP40 octamers are essential for Ebola virus replication. Hoenen, T., Volchkov, V., Kolesnikova, L., Mittler, E., Timmins, J., Ottmann, M., Reynard, O., Becker, S., Weissenhorn, W. J. Virol. (2005) [Pubmed]
  11. Development, characterization and use of monoclonal VP40-antibodies for the detection of Ebola virus. Lucht, A., Grunow, R., Möller, P., Feldmann, H., Becker, S. J. Virol. Methods (2003) [Pubmed]
  12. Effects of Ebola virus glycoproteins on endothelial cell activation and barrier function. Wahl-Jensen, V.M., Afanasieva, T.A., Seebach, J., Ströher, U., Feldmann, H., Schnittler, H.J. J. Virol. (2005) [Pubmed]
  13. Ebola virus VP40-induced particle formation and association with the lipid bilayer. Jasenosky, L.D., Neumann, G., Lukashevich, I., Kawaoka, Y. J. Virol. (2001) [Pubmed]
  14. Nedd4 regulates egress of Ebola virus-like particles from host cells. Yasuda, J., Nakao, M., Kawaoka, Y., Shida, H. J. Virol. (2003) [Pubmed]
  15. Virus-like particles exhibit potential as a pan-filovirus vaccine for both Ebola and Marburg viral infections. Swenson, D.L., Warfield, K.L., Negley, D.L., Schmaljohn, A., Aman, M.J., Bavari, S. Vaccine (2005) [Pubmed]
  16. Effect of Ebola virus proteins GP, NP and VP35 on VP40 VLP morphology. Johnson, R.F., Bell, P., Harty, R.N. Virol. J. (2006) [Pubmed]
  17. Analysis of Ebola virus and VLP release using an immunocapture assay. Kallstrom, G., Warfield, K.L., Swenson, D.L., Mort, S., Panchal, R.G., Ruthel, G., Bavari, S., Aman, M.J. J. Virol. Methods (2005) [Pubmed]
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