HIV-1 Gag protein associates with F-actin present in microfilaments.
Several studies have provided evidence that the cellular cytoskeleton may be involved in the assembly and budding of retroviruses. In fractionation studies of HIV-1-infected CEM cells, the majority of the unprocessed Gag polyprotein cofractionated with the cellular cytoskeleton. In vivo and in vitro analyses of this interaction indicated that the unprocessed Gag polyprotein is capable of association with polymerized actin (F-actin). Binding of Gag to F-actin may be involved in the assembly or budding of HIV-1.
Rey
O
O
Department of Pediatrics, School of Medicine, University of California at Los Angeles 90095, USA. <orey@pediatrics.medsch.ucla.edu>
Canon
J
J
Krogstad
P
P
D008841:Actin Cytoskeleton / Q000378:metabolism* / Q000821:virology; D000199:Actins / Q000378:metabolism*; D000818:Animals; D002460:Cell Line; D002461:Cell Line, Transformed; D002522:Chlorocebus aethiops; D015683:Gene Products, gag / Q000378:metabolism*; D015497:HIV-1 / Q000502:physiology*; D006801:Humans; D011485:Protein Binding; D019065:Virus Assembly
D000199:Actins; D015683:Gene Products, gag