Abstract
Domains have been identified in the Gag proteins of a number of retroviruses, and in the matrix proteins of the rhabdoviruses and filoviruses, that play a critical role in the pinching off of virus particles from the plasma membrane. These sequences are collectively termed late or L domains to reflect their function late in the virus budding process. One of the intriguing features of these L domains is that they all contain highly conserved motifs known to mediate protein-protein interactions between cellular proteins. Three classes of motifs have been defined in viral L domains: PTAP, PPXY, and YXXL. In each case, the integrity of these motifs appears to be essential for L domain activity, suggesting that L domains function by interacting with a host factor(s). This minireview summarizes the present state of our knowledge concerning viral L domain function and describes recent tantalizing clues regarding the identity of the cellular partners with which L domains interact.
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