title: Distal leucines are key functional determinants of Alix-binding simian immunodeficiency virus SIV(smE543) and SIV(mac239) type 3 L domains.
abstract: In addition to PTAP L domains, primate lentiviruses carry Alix-binding motifs that include the recently described type 3 SREKPYKEVTEDLLHLNSLF sequence. We examined the requirements for the type 3 sequence motif in simian immunodeficiency virus SIV(smE543) and identified the (499)LNSLF(503) sequence as a key functional determinant. Mutation of distal leucines (499)L and (502)L (LL mutant) caused an inhibitory effect on Alix-dependent SIV(smE543) release that was quantitatively similar to that observed following disruption of the type 3 L domain or RNA interference (RNAi) depletion of Alix. Similar results were obtained with the SIV(mac239) LL mutant. Thus, distal leucines are key determinants of SIV(smE543) and SIV(mac239) type 3 L domains.
authors.affiliation: Laboratory of Molecular Microbiology, NIAID, NIH, 4 Center Drive, Bethesda, MD 20892, USA.
authors.forename: Nana F
authors.initials: NF
authors.lastname: Bello
authors.forename: Fan
authors.initials: F
authors.lastname: Wu
authors.forename: Paola
authors.initials: P
authors.lastname: Sette
authors.forename: Vincent
authors.initials: V
authors.lastname: Dussupt
authors.forename: Vanessa M
authors.initials: VM
authors.lastname: Hirsch
authors.forename: Fadila
authors.initials: F
authors.lastname: Bouamr
mesh_terms: D020816:Amino Acid Motifs; D019943:Amino Acid Substitution / Q000235:genetics; D002135:Calcium-Binding Proteins / Q000378:metabolism*; D054884:Host-Pathogen Interactions; D007930:Leucine / Q000235:genetics; D011485:Protein Binding; D015302:Simian Immunodeficiency Virus / Q000502:physiology*; D014764:Viral Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D057074:Virus Release
chemical_list: D002135:Calcium-Binding Proteins; D014764:Viral Proteins; D007930:Leucine