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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

Authors :
Tsutomu Murakami
Yuko Futahashi
Yuko Morikawa
Naoki Yamamoto
Jun Komano
Emiko Urano
Toru Aoki
Source :
The Journal of General Virology
Publication Year :
2008
Publisher :
Microbiology Society, 2008.

Abstract

The matrix domain (MA) of human immunodeficiency virus type 1 Pr55Gagis 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.

Details

ISSN :
14652099 and 00221317
Volume :
89
Database :
OpenAIRE
Journal :
Journal of General Virology
Accession number :
edsair.doi.dedup.....27dbf7a8424cc3fca84d383dbe97cabe