Evidence map›Paper›PMID 18657842›Full record

ArticleVirology2008

Suboptimal inhibition of protease activity in human immunodeficiency virus type 1: effects on virion morphogenesis and RNA maturation.

Michael D Moore, William Fu, Ferri Soheilian, Kunio Nagashima, Roger G Ptak, Vinay K Pathak, Wei-Shau Hu

Open access · greenAbstract read
In one paragraph

Article in Virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.8field-weighted citation impact, top 32% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Neutral sphingomyelinase 2 is required for HIV-1 maturation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  3. Article
  4. Article
  5. Maturation of retroviruses.Current opinion in virology · 2019
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Allosteric integrase inhibitor potency is determined through the inhibition of HIV-1 particle maturation.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Michael D MooreHIV Drug Resistance Program, National Cancer Institute at Frederick, P.O. Box B, Building 535, Room 336, Frederick, Maryland 21702, USA.
William Fu
Ferri Soheilian
Kunio Nagashima
Roger G Ptak
Vinay K Pathak
Wei-Shau Hu
Frederick National Laboratory for Cancer Research · USScience Applications International Corporation (United States) · US

Funding

Understanding the Pseudodiploidy of the Retroviral GenomeZIABC010814 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI HU, WEI-SHAU · 2009 to 2025
$12.3M
Understanding Retroviral Gag and RNA Targeting and Virus AssemblyZIABC010506 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI HU, WEI-SHAU · 2009 to 2025
$12.1M
Virus Assembly, RNA Packaging, and ReplicationZ01BC010506 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI HU, WEI-SHAU · 2003 to 2008
$819k
Role of Connection and RNase H Domains of HIV-1 RT in Antiviral Drug ResistanceZIABC010532 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI PATHAK, VINAY K. · 2009 to 2011
$640k
Intramural NIH HHS Z01 BC010506NCI NIH HHS N01 CO012400NCI NIH HHS N01-CO-12400
6 · The paper itself

Abstract

Protease activity within nascently released human immunodeficiency virus type 1 (HIV-1) particles is responsible for the cleavage of the viral polyproteins Gag and Gag-Pol into their constituent parts, which results in the subsequent condensation of the mature conical core surrounding the viral genomic RNA. Concomitant with viral maturation is a conformational change in the packaged viral RNA from a loosely associated dimer into a more thermodynamically stable form. In this study we used suboptimal concentrations of two protease inhibitors, lopinavir and atazanavir, to study their effects on Gag polyprotein processing and on the properties of the RNA in treated virions. Analysis of the treated virions demonstrated that even with high levels of inhibition of viral infectivity (IC(90)), most of the Gag and Gag-Pol polyproteins were processed, although slight but significant increases in processing intermediates of Gag were detected. Drug treatments also caused a significant increase in the proportion of viruses displaying either immature or aberrant mature morphologies. The aberrant mature particles were characterized by an electron-dense region at the viral periphery and an electron-lucent core structure in the viral center, possibly indicating exclusion of the genomic RNA from these viral cores. Intriguingly, drug treatments caused only a slight decrease in overall thermodynamic stability of the viral RNA dimer, suggesting that the dimeric viral RNA was able to mature in the absence of correct core condensation.

Indexed as

Atazanavir SulfateDimerizationgag Gene Products, Human Immunodeficiency VirusHIV-1HIV ProteaseHIV Protease InhibitorsHumansLopinavirMicroscopy, Electron, TransmissionOligopeptidesPyridinesPyrimidinonesRNA, ViralVirionAtazanavir Sulfategag Gene Products, Human Immunodeficiency VirusHIV ProteaseHIV Protease InhibitorsLopinavirOligopeptidesp16 protease, Human immunodeficiency virus 1PyridinesPyrimidinonesRNA, Viral

Identifiers

PMID18657842
PMCPMC2577075
OpenAlexW2035182404

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.