Disease relevance of VP40

• Last, these studies imply that VP40 likely plays an important role in filovirus budding, and that budding of retroviruses, rhabdoviruses, and filoviruses may proceed via analogous mechanisms [1].
• Expression of VP40 in Escherichia coli and subsequent proteolysis yielded two structural variants differing by a C-terminal truncation 114 amino acid residues long [2].
• Ebola virus particle formation and budding are mediated by the VP40 protein, which possesses overlapping PTAP and PPXY late domain motifs (7-PTAPPXY-13) [3].
• Recombinant baculoviruses (rBV) expressing Ebola virus VP40 (rBV-VP40) or GP (rBV-GP) proteins were generated [4].
• The structure/function of influenza virus M1 will be compared with that of the Ebola virus matrix protein, VP40 [5].

High impact information on VP40

• VP40, the putative matrix protein of both Ebola and Marburg viruses, possesses a conserved proline-rich motif (PY motif) at its N terminus [1].
• VP40 octamers are essential for Ebola virus replication [6].
• These results suggest that RNA binding of VP40 and therefore octamer formation are essential for the Ebola virus life cycle [6].
• The VP40 matrix protein of Ebola virus buds from cells in the form of virus-like particles (VLPs) and plays a central role in virus assembly and budding [7].
• Contribution of ebola virus glycoprotein, nucleoprotein, and VP24 to budding of VP40 virus-like particles [7].

Biological context of VP40

• Together, these results provide strong evidence that Ebola virus VP40 is sufficient for virus assembly and budding from the plasma membrane [8].

Anatomical context of VP40

• We confirmed previous findings that truncation of the 50 C-terminal amino acids of VP40 results in decreased association with cellular membranes and demonstrated that this deletion disrupts hydrophobic interactions of VP40 with the lipid bilayer, as well as abolishing particle formation [9].

Associations of VP40 with chemical compounds

• In addition, we find that full-length VP40 [VP40(1-326)] and VP40(31-326) are both released into the cell culture supernatant and float up in sucrose gradients [8].

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 [10].

Other interactions of VP40

• Effect of Ebola virus proteins GP, NP and VP35 on VP40 VLP morphology [10].

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 [10].
• Ebola virus VP40 late domains are not essential for viral replication in cell culture [3].
• Sequence analysis of the GP, NP, VP40 and VP24 genes of Ebola virus isolated from deceased, surviving and asymptomatically infected individuals during the 1996 outbreak in Gabon: comparative studies and phylogenetic characterization [11].

References