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We have demonstrated that COS7 cells transiently co-expressing myristylation-defective (Myr ) and protease-defective (PR ) human immunodeficiency virus (HIV) mutants can release infectious virions when co-transfected with an amphotropic murine leukaemia virus envelope protein expression plasmid (SV-A-MLV-env). In contrast, no infectious virions were detected when a PR, noninfectious HIV gag mutant was co-expressed with the Myr mutant, although the Myr mutant could still process the immature core particles in trans. This result indicates that generation of functionally normal Gag proteins is required for virus infectivity in our complementation system. A mutant with a 56- amino-acid deletion in the N-terminal region of the capsid (CA) domain could still complement the PR mutant to generate infectious virions, suggesting that the deletion mutant could provide a functional protease for processing in the PR mutant. This result is consistent with the concept that mutations within the N-terminal region of the CA domain have no major effects on Gag-Pol incorporation into particles.
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