Basic Residues in the Matrix Domain and Multimerization Target Murine Leukemia Virus Gag to the Virological Synapse

摘要: Murine leukemia virus (MLV) can efficiently spread in tissue cultures by polarizing assembly to virological synapses. The viral envelope glycoprotein (Env) establishes cell-cell contacts and subsequently recruits Gag a process that depends on its cytoplasmic tail. MLV is recruited synapses through the matrix domain (MA) (J. Jin, F. Li, W. Mothes, J. Virol. 85:7672-7682, 2011). However, how MA targets sites of contact remains unknown. Here we report basic residues within are critical for directing Alternative membrane targeting domains (MTDs) containing multiple substitute direct polarized assembly. Similarly, mutations polybasic cluster disrupt polarization be rescued N-terminal addition MTDs residues. alone fail targeted synapse. Systematic deletion experiments reveal known mediate multimerization also required. Thus, our data predict existence specific "acidic" interface at mediates recruitment via multimerization.