Evidence map›Paper›PMID 36601299›Full record

ArticleVirus evolution2022

The evolution of the HIV-1 protease folding stability.

David Ferreiro, Ruqaiya Khalil, María J Gallego, Nuno S Osorio, Miguel Arenas

Abstract read
In one paragraph

Article in Virus evolution, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
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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

5 authors.

David FerreiroCINBIO, Universidade de Vigo, Vigo 36310, Spain.
Ruqaiya KhalilCINBIO, Universidade de Vigo, Vigo 36310, Spain.
María J GallegoCINBIO, Universidade de Vigo, Vigo 36310, Spain.
Nuno S OsorioLife and Health Sciences Research Institute, School of Medicine, University of Minho, Braga 4710-057, Portugal.ORCID https://orcid.org/0000-0003-0949-5399
Miguel ArenasCINBIO, Universidade de Vigo, Vigo 36310, Spain.ORCID https://orcid.org/0000-0002-0516-2717

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The evolution of structural proteins is generally constrained by the folding stability. However, little is known about the particular capacity of viral proteins to accommodate mutations that can potentially affect the protein stability and, in general, the evolution of the protein stability over time. As an illustrative model case, here, we investigated the evolution of the stability of the human immunodeficiency virus (HIV-1) protease (PR), which is a common HIV-1 drug target, under diverse evolutionary scenarios that include (1) intra-host virus evolution in a cohort of seventy-five patients sampled over time, (2) intra-host virus evolution sampled before and after specific PR-based treatments, and (3) inter-host evolution considering extant and ancestral (reconstructed) PR sequences from diverse HIV-1 subtypes. We also investigated the specific influence of currently known HIV-1 PR resistance mutations on the PR folding stability. We found that the HIV-1 PR stability fluctuated over time within a constant and wide range in any studied evolutionary scenario, accommodating multiple mutations that partially affected the stability while maintaining activity. We did not identify relationships between change of PR stability and diverse clinical parameters such as viral load, CD4

Indexed as

HIV-1 proteaseprotease inhibitorsprotein evolutionprotein folding stabilityresistance mutations

Identifiers

PMID36601299
PMCPMC9802575

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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.