Disease relevance of VP40

• VP40-containing MVBs were free of nucleocapsids [1].
• VP40 is functionally homologous to the matrix proteins of other nonsegmented negative-strand RNA viruses [2].

High impact information on VP40

• Furthermore, VP24 displayed membrane-binding properties and was recruited into filamentous virus-like particles (VLPs) that are induced by VP40 [2].
• The majority of VP40-positive membranes were first detected comigrating with small vesicles [3].
• The inhibition of intracellular vesicular trafficking by monensin significantly reduced the appearance of VP40 at the plasma membrane [3].
• The Marburg virus (MARV) envelope consists of a lipid membrane and two major proteins, the matrix protein VP40 and the glycoprotein GP [4].
• Upon coexpression with VP40, GP is redistributed from the trans-Golgi network into the VP40-containing MVBs [4].

Anatomical context of VP40

• Finally, VP40 appeared in a patch-like pattern beneath the plasma membrane [3].
• Our data indicate that MBGV VP40 was able to interact with membranes of late endosomes in the course of viral infection [1].
• Additionally, VP40 was identified in the foci of virus-induced membrane proliferation and in intracellular membrane clusters which had the appearance of multivesicular bodies (MVBs) [1].
• We suggest that VP40, which is capable of interacting with viral nucleocapsids, provides an interface of MARV subviral particles and filopodia [5].

Associations of VP40 with chemical compounds

• Blocking of protein synthesis by use of cycloheximide at the time when VP40 was mainly associated with the small vesicles did not prevent the redistribution of VP40 to the late endosomes and further to the plasma membrane [3].

Other interactions of VP40

• These fragments were found to encode the VP35 and VP40 proteins [6].

Analytical, diagnostic and therapeutic context of VP40

• Localization of VP40 in Marburg virus (MBGV)-infected cells was studied by using immunofluorescence and immunoelectron microscopic analysis [1].

References