The polybasic region is not essential for membrane binding of the matrix protein M1 of influenza virus.
The matrix protein M1, the organizer of assembly of influenza virus, interacts with other virus components and with cellular membranes. It has been proposed that M1 binding to lipids is mediated by its polybasic region, but this could hitherto not been investigated in vivo since M1 accumulates in the nucleus of transfected cells. We have equipped M1 with nuclear export signals and showed that the constructs are bound to cellular membranes. Exchange of the complete polybasic region and of further hydrophobic amino acids in its vicinity did not prevent association of M1 with membranes. We therefore suppose that M1 probably interacts with membranes via multiple binding sites.
Thaa
Bastian
B
Department of Immunology and Molecular Biology Veterinary Faculty, Free University Berlin, Philippstr. 13, 10115 Berlin, Germany.
Herrmann
Andreas
A
Veit
Michael
M
D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism*; D009980:Influenza A virus / Q000502:physiology*; D008958:Models, Molecular; D049790:Nuclear Export Signals; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D014763:Viral Matrix Proteins / Q000235:genetics / Q000378:metabolism*
C488936:M1 protein, Influenza A virus; D049790:Nuclear Export Signals; D011994:Recombinant Proteins; D014763:Viral Matrix Proteins