In summary, we show the modulatory role of Gag on envelope association with lipid enriched micro domain that play an important role in transmission by modulating envelope assembly onto virus particles in primary CD4 + T cells. Despite its close proximity, DRMs isolated from cells may not necessarily represent the preexisting rafts in living cells. [34, 35] . Hence, GPI anchored proteins because of their raftofilcity often are regarded as best choice for studying raft association and targeting [36] . In our present study, in addition to investigate role of gag in envelope association with DRM, we attempted to look into GPI-anchored proteins for their high affinity towards lipid raft association [35, 37] . The lipidbinding B subunit of cholera toxin (CTxB), recognizing GM1 at cell surface in plasma membrane, was used to study the envelope transport into lipid rafts. Like other GPI-anchored proteins, these markers were also known to be associated with DRM [38] . Our data showed that abrogation of Gag-Env interaction down modulated envelope transport into CD59 positive compartment in primary CD4 + T cells and also failed to associate with DRM fractions. While viral precursors Gag and Gag-Pol are synthesized by polysomes in cellular cytoplasm, the oligomeric envelope protein is synthesized in endoplasmic reticulum and post-translationally modulated in the Golgi apparatus, traverses into the secretory pathway towards assembling onto budding virions. We envisage that Gag by acting as cargo transport intermediate carry envelope protein through trans-golgi route sorting into domains of lipid rich plasma membrane enable them assemble onto budding virions in primary CD4 + T cells.