RT Journal Article SR Electronic(1) A1 Urano, Emiko A1 Aoki, Toru A1 Futahashi, Yuko A1 Murakami, Tsutomu A1 Morikawa, Yuko A1 Yamamoto, Naoki A1 Komano, JunYR 2008 T1 Substitution of the myristoylation signal of human immunodeficiency virus type 1 Pr55Gag with the phospholipase C-δ1 pleckstrin homology domain results in infectious pseudovirion production JF Journal of General Virology, VO 89 IS 12 SP 3144 OP 3149 DO https://doi.org/10.1099/vir.0.2008/004820-0 PB Microbiology Society, SN 1465-2099, AB The matrix domain (MA) of human immunodeficiency virus type 1 Pr55Gag is covalently modified with a myristoyl group that mediates efficient viral production. However, the role of myristoylation, particularly in the viral entry process, remains uninvestigated. This study replaced the myristoylation signal of MA with a well-studied phosphatidylinositol 4,5-biphosphate-binding plasma membrane (PM) targeting motif, the phospholipase C-δ1 pleckstrin homology (PH) domain. PH–Gag–Pol PM targeting and viral production efficiencies were improved compared with Gag–Pol, consistent with the estimated increases in Gag–PM affinity. Both virions were recovered in similar sucrose density-gradient fractions and had similar mature virion morphologies. Importantly, PH–Gag–Pol and Gag–Pol pseudovirions had almost identical infectivity, suggesting a dispensable role for myristoylation in the virus life cycle. PH–Gag–Pol might be useful in separating the myristoylation-dependent processes from the myristoylation-independent processes. This the first report demonstrating infectious pseudovirion production without myristoylated Pr55Gag., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.2008/004820-0