The three-dimensional solution structure of the matrix protein from the type D retrovirus, the Mason-Pfizer monkey virus, and implications for the morphology of retroviral assembly.
The Mason-Pfizer monkey virus (M-PMV) is the prototype of the type D retroviruses. In type B and D retroviruses, the Gag protein pre-assembles before association with the membrane, whereas in type C retroviruses (lentiviruses, BLV/HTLV group) Gag is targeted efficiently to the plasma membrane, where the particle formation occurs. The N-terminal domain of Gag, the matrix protein (MA), plays a critical role in determining this morphogenic difference. We have determined the three-dimensional solution structure of the M-PMV MA by heteronuclear nuclear magnetic resonance. The protein contains four alpha-helices that are structurally similar to the known type C MA structures. This similarity implies possible common assembly units and membrane-binding mechanisms for type C and B/D retroviruses. In addition to this, the interpretation of mutagenesis data has enabled us to identify, for the first time, the structural basis of a putative intracellular targeting motif.
Conte
M R
MR
Department of Biochemistry, Imperial College of Science, Technology and Medicine, University of London, London SW7 2AY, UK.
Klikova
M
M
Hunter
E
E
Ruml
T
T
Matthews
S
S
D002462:Cell Membrane / Q000821:virology; D004926:Escherichia coli; D015683:Gene Products, gag / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D016093:Mason-Pfizer monkey virus / Q000648:ultrastructure; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012996:Solutions; D014763:Viral Matrix Proteins / Q000737:chemistry*
D015683:Gene Products, gag; D012996:Solutions; D014763:Viral Matrix Proteins