HIV-1 protease with leucine zipper fused at N-terminus exhibits enhanced linker amino acid-dependent activity
Abstract Background HIV-1 protease (PR) activation is triggered by Gag-Pol dimerization. Premature PR activation results in reduced virion yields due to enhanced Gag cleavage. A p6* transframe peptide located directly upstream of protease is believed to play a modulating role in PR activation. Previ...
Main Authors: | Fu-Hsien Yu, Chin-Tien Wang |
---|---|
Format: | Article |
Language: | English |
Published: |
BMC
2018-04-01
|
Series: | Retrovirology |
Subjects: | |
Online Access: | http://link.springer.com/article/10.1186/s12977-018-0413-6 |
Similar Items
-
Effects of reduced gag cleavage efficiency on HIV-1 Gag-Pol package
by: Yi-Ru Lin, et al.
Published: (2022-04-01) -
HIV-1 Mutant Assembly, Processing and Infectivity Expresses Pol Independent of Gag
by: Fu-Hsien Yu, et al.
Published: (2020-01-01) -
The prototype foamy virus protease is active independently of the integrase domain
by: Spannaus Ralf, et al.
Published: (2012-05-01) -
Human Immunodeficiency Virus gag and protease: partners in resistance
by: Fun Axel, et al.
Published: (2012-08-01) -
Pharmacological intervention of HIV-1 maturation
by: Dan Wang, et al.
Published: (2015-11-01)