The structural precursor polyprotein, Gag, encoded by all retroviruses, including the human immunodeficiency virus type 1 (HIV-1), is necessary and sufficient for the assembly and release of particles that morphologically resemble immature virus particles. Previous studies have shown that the addition of Ca 2+ to cells expressing Gag enhances virus particle production. However, no specific cellular factor has been implicated as mediator of Ca 2+ provision. The inositol (1,4,5)-triphosphate receptor (IP3R) gates intracellular Ca 2+ stores. Following activation by binding of its ligand, IP3, it releases Ca 2+ from the stores.

We demonstrate here that IP3R function is required for efficient release of HIV-1 virus particles. Depletion of IP3R by small interfering RNA, sequestration of its activating ligand by expression of a mutated fragment of IP3R that binds IP3 with very high affinity, or blocking formation of the ligand by inhibiting phospholipase C-mediated hydrolysis of the precursor, phosphatidylinositol-4,5-biphosphate, inhibited Gag particle release. These disruptions, as well as interference with ligand-receptor interaction using antibody targeted to the ligand-binding site on IP3R, blocked plasma membrane accumulation of Gag.

These findings identify IP3R as a new determinant in HIV-1 trafficking during Gag assembly and introduce IP3R-regulated Ca 2+ signaling as a potential novel cofactor in viral particle release. Assembly of the human immunodeficiency virus (HIV) is determined by a single gene that encodes a structural polyprotein precursor, Gag (), and may occur at the plasma membrane or within late endosomes/multivesicular bodies (LE/MVB) (,,; reviewed in reference ). Irrespective of where assembly occurs, the assembled particle is released from the plasma membrane of the host cell. Release of Gag as virus- like particles (VLPs) requires the C-terminal p6 region of the protein (, ), which contains binding sites for Alix (, ) and Tsg101 (,,,,, ). Efficient release of virus particles requires Gag interaction with Alix and Tsg101. Alix and Tsg101 normally function to sort cargo proteins to LE/MVB for lysosomal degradation (,,, ). Previous studies have shown that addition of ionomycin, a calcium ionophore, and CaCl 2 to the culture medium of cells expressing Gag or virus enhances particle production (, ).

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