Open AccessStructural studies on the Ebola virus matrix protein VP40 indicate that matrix proteins of enveloped RNA viruses are analogues but not homologues
Author(s) -
Timmins Joanna,
Ruigrok Rob W.H.,
Weissenhorn Winfried
Publication year - 2004
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2004.tb09480.x
Subject(s) - vp40 , viral matrix protein , ebola virus , vesicular stomatitis virus , biology , viral envelope , virology , virus , microbiology and biotechnology , rna virus , rna , viral structural protein , viral entry , viral replication , genetics , gene
Matrix proteins are the driving force of assembly of enveloped viruses. Their main function is to interact with and polymerize at cellular membranes and link other viral components to the matrix–membrane complex resulting in individual particle shapes and ensuring the integrity of the viral particle. Although matrix proteins of different virus families show functional analogy, they share no sequence or structural homology. Their diversity is also evident in that they use a variety of late domain motifs to commit the cellular vacuolar protein sorting machinery to virus budding. Here, we discuss the structural and functional aspects of the filovirus matrix protein VP40 and compare them to other known matrix protein structures from vesicular stomatitis virus, influenza virus and retroviral matrix proteins.