Measles virus M and F proteins associate with detergent-resistant membrane fractions and promote formation of virus-like particles.
Assembly and release of particles comprise a late step in virus-host cell interactions. Though it may share major biological properties with its orthologues in related viruses, trafficking and oligomerization of the matrix (M) protein of Measles virus (MV) and its relative contribution to assembly and budding of particles from particular host cells have not been addressed in more detail. Plasmid-driven expression of authentic and mutant M proteins revealed that the amino acid at position 89, an important adaptation determinant for growth of attenuated strains in Vero cells, influences the electrophoretic mobility but not the intracellular distribution of M proteins, nor their ability to oligomerize or migrate as a doublet band in SDS-PAGE. M proteins were found to co-float with detergent-resistant membrane fractions (DRM) and this was enhanced upon co-expression of the F protein. In contrast to their DRM association, the ability of M proteins to promote release of virus-like particles (VLPs) was not affected by the presence of F proteins, which on their own also efficiently promoted VLP production. Thus, DRM recruitment of MV F and M proteins and their ability to drive particle formation are not correlated.
Pohl
Christine
C
Institute for Virology and Immunobiology, University of Wuerzburg, Versbacher Str. 7, D-97078 Wuerzburg, Germany.
Duprex
W Paul
WP
Centre for Cancer Research and Cell Biology, School of Biomedical Sciences, The Queen's University of Belfast, Belfast BT9 7BL, Northern Ireland, UK.
Krohne
Georg
G
Department for Electron Microscopy, University Wuerzburg, Biocenter, D-97078 Wuerzburg, Germany.
Rima
Bertus K
BK
Centre for Cancer Research and Cell Biology, School of Biomedical Sciences, The Queen's University of Belfast, Belfast BT9 7BL, Northern Ireland, UK.
Schneider-Schaulies
Sibylle
S
Institute for Virology and Immunobiology, University of Wuerzburg, Versbacher Str. 7, D-97078 Wuerzburg, Germany.
D019943:Amino Acid Substitution; D002458:Cell Fractionation; D002462:Cell Membrane / Q000378:metabolism*; D047468:Immunoprecipitation; D008459:Measles virus / Q000235:genetics / Q000502:physiology*; D046529:Microscopy, Electron, Transmission; D008856:Microscopy, Fluorescence; D014760:Viral Fusion Proteins / Q000235:genetics / Q000378:metabolism*; D014763:Viral Matrix Proteins / Q000235:genetics / Q000378:metabolism*; D019065:Virus Assembly / Q000235:genetics
D014760:Viral Fusion Proteins; D014763:Viral Matrix Proteins