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

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Abstract
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 α‐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.

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