About: Placement of Leucine Zipper Motifs at the Carboxyl Terminus of HIV-1 Protease Significantly Reduces Virion Production

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About: Placement of Leucine Zipper Motifs at the Carboxyl Terminus of HIV-1 Protease Significantly Reduces Virion Production Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Placement of Leucine Zipper Motifs at the Carboxyl Terminus of HIV-1 Protease Significantly Reduces Virion Production
Creator	Chiang, K-J Huang, S-M Wang, C-C Wang, Y-Y
Source	PMC
abstract	Natural HIV-1 protease (PR) is homodimeric. Some researchers believe that interactions between HIV-1 Gag-Pol molecules trigger the activation of embedded PR (which mediates Gag and Gag-Pol cleavage), and that Gag-Pol assembly domains outside of PR may contribute to PR activation by influencing PR dimer interaction in a Gag-Pol context. To determine if the enhancement of PR dimer interaction facilitates PR activation, we placed single or tandem repeat leucine zippers (LZ) at the PR C-terminus, and looked for a correlation between enhanced Gag processing efficiency and increased Gag-PR-LZ multimerization capacity. We found significant reductions in virus-like particles (VLPs) produced by HIV-1 mutants, with LZ fused to the end of PR as a result of enhanced Gag cleavage efficiency. Since VLP production can be restored to wt levels following PR activity inhibition, this assembly defect is considered PR activity-dependent. We also found a correlation between the LZ enhancement effect on Gag cleavage and enhanced Gag-PR multimerization. The results suggest that PR dimer interactions facilitated by forced Gag-PR multimerization lead to premature Gag cleavage, likely a result of premature PR activation. Our conclusion is that placement of a heterologous dimerization domain downstream of PR enhances PR-mediated Gag cleavage efficiency, implying that structural conformation, rather than the primary sequence outside of PR, is a major determinant of HIV-1 PR activation.
has issue date	2012-03-01(xsd:dateTime)
bibo:doi	10.1371/journal.pone.0032845
bibo:pmid	22396796
has license	cc-by
sha1sum (hex)	3e035bd3c87d15ec4bca05cd13551c70d1bc5e78
schema:url	https://doi.org/10.1371/journal.pone.0032845
resource representing a document's title	Placement of Leucine Zipper Motifs at the Carboxyl Terminus of HIV-1 Protease Significantly Reduces Virion Production
has PubMed Central identifier	PMC3291649
has PubMed identifier	22396796
schema:publication	PLoS One
resource representing a document's body	covid:3e035bd3c87d15ec4bca05cd13551c70d1bc5e78#body_text
is schema:about of	named entity 'PRODUCTION' named entity 'CARBOXYL' named entity 'Gag' named entity 'homodimeric' named entity 'Our' named entity 'enhanced' named entity 'dimerization' named entity 'enhanced' named entity 'domain' named entity 'cleavage' named entity 'HETEROLOGOUS' named entity 'RESULTS' named entity 'DIMERIZATION' named entity 'PRIMARY' named entity 'ASSEMBLY' named entity 'CONFORMATION' named entity 'PLACED' named entity 'SEQUENCE' named entity 'DOWNSTREAM' named entity 'SINGLE' named entity 'REDUCTIONS' named entity 'VIRUS-LIKE PARTICLES' named entity 'FOUND' named entity 'INTERACTION' named entity 'LEVELS' named entity 'AS A RESULT OF' named entity 'MUTANTS' named entity 'GAG' named entity 'CONSIDERED' named entity 'RESEARCHERS' named entity 'CONTEXT' named entity 'DOMAIN' named entity 'EFFECT' named entity 'FORCED' named entity 'EFFICIENCY' named entity 'DEPENDENT' named entity 'HIV-1' named entity 'CORRELATION' named entity 'ACTIVITY' named entity 'C-TERMINUS' named entity 'DIMER' named entity 'OUR' named entity 'ENHANCED' named entity 'HIV-1 PROTEASE' named entity 'LEUCINE ZIPPER' named entity 'LIKELY' named entity 'RATHER' named entity 'IS A' named entity 'SUGGEST' named entity 'INHIBITION' named entity 'DETERMINE' named entity 'PRODUCTION' named entity 'NATURAL' named entity 'END' named entity 'PLACEMENT' named entity 'HIV-1 PROTEASE' named entity 'TERMINUS' named entity 'LEAD' named entity 'SIGNIFICANT' named entity 'CLEAVAGE' named entity 'CONCLUSION' named entity 'OUTSIDE' named entity 'TRIGGER' named entity 'BELIEVE' named entity 'A MAJOR' named entity 'MULTIMERIZATION' named entity 'PROCESSING' named entity 'VLP' named entity 'MOLECULES' named entity 'INCREASED' named entity 'CONTRIBUTE ' named entity 'ACTIVATION' named entity 'PREMATURE' named entity 'MOTIFS' named entity 'INTERACTIONS' named entity 'RESULT' named entity 'GAG-POL' named entity 'FUSED TO'

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