Journal
PLOS ONE
Volume 17, Issue 1, Pages -Publisher
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0262477
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Categories
Funding
- Taipei Veterans General Hospital [V106C-047, V107C-049, V108C034]
- Taiwan Ministry of Science and Technology [106-2320-B-010-017-MY2, 1082320-B-010-030]
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The p6* region in HIV-1 Gag-Pol plays a crucial role in PR activation. Mutations at p6* F8 result in reduced virus infectivity due to impaired PR maturation and RT packaging.
A transframe region within HIV-1 Gag-Pol (referred to as p6* or p6pol), directly linked to the protease (PR) N-terminus, plays a pivotal role in modulating PR activation. To identify specific p6* residues involved in PR activation, we created a series of p6* mutants by making substitutions for conserved p6* residues. Our results indicate that some p6* mutants were defective in terms of virus infectivity, despite displaying a wild-type virus particle processing pattern. Mutations at p6* F8 reduced virus infectivity associated with insufficient virus processing, due in part to impaired PR maturation and RT packaging. Our data strongly suggest that conserved Phe (F) residues at position 8 of p6* are involved in the PR maturation process.
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