The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Matrix protein. Forms the spherical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. Binds strongly to viral nucleic acids and promote their aggregation. Also destabilizes the nucleic acids duplexes via highly structured zinc-binding motifs. Homodimer; the homodimers are part of the immature particles. Interacts with host NEDD4; these interactions are essential for budding and release of viral particles. Homodimer; further assembles as homohexamers. Late-budding domains (L domains) are short sequence motifs essential for viral particle release. They can occur individually or in close proximity within structural proteins. They interacts with sorting cellular proteins of the multivesicular body (MVB) pathway. Most of these proteins are class E vacuolar protein sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes. Matrix protein p15 contains one L domain: a PPXY motif which binds to the WW domains of the ubiquitin ligase NEDD4. The capsid protein N-terminus seems to be involved in Gag-Gag interactions. Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation. Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and is required for the assembly of viral particles. Produced by conventional translation.