HIV-1 is a retrovirus that relies on myristoylation of one of its structural proteins in order to successfully package its genome, assemble and mature into a new infectious particle. Viral matrix protein, the N-terminal–most domain of the gag polyprotein, is myristoylated. This myristoylation modification targets gag to the membrane of the host cell. Utilizing the myristoyl-electrostatic switch, including a basic patch on the matrix protein, gag can assemble at lipid rafts at the plasma membrane for viral assembly, budding and further maturation.  In order to prevent viral infectivity, myristoylation of the matrix protein could become a good drug target.