Evidence map›Paper›PMID 35192358›Full record

ArticleJournal of proteome research2022

Discovery of Dehydroamino Acid Residues in the Capsid and Matrix Structural Proteins of HIV-1.

Rachel M Miller, Rachel A Knoener, Bayleigh E Benner, Brian L Frey, Mark Scalf, Michael R Shortreed, Nathan M Sherer, Lloyd M Smith

Abstract read
In one paragraph

Article in Journal of proteome research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
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

8 authors.

Rachel M MillerDepartment of Chemistry, University of Wisconsin, 1101 University Avenue, Madison, Wisconsin 53706, United States.ORCID 0000-0003-1461-6386
Rachel A KnoenerDepartment of Chemistry, University of Wisconsin, 1101 University Avenue, Madison, Wisconsin 53706, United States.
Bayleigh E BennerMcArdle Laboratory for Cancer Research and Institute for Molecular Virology, University of Wisconsin, Madison, Wisconsin 53705, United States.
Brian L FreyDepartment of Chemistry, University of Wisconsin, 1101 University Avenue, Madison, Wisconsin 53706, United States.ORCID 0000-0002-0397-7269
Mark ScalfDepartment of Chemistry, University of Wisconsin, 1101 University Avenue, Madison, Wisconsin 53706, United States.
Michael R ShortreedDepartment of Chemistry, University of Wisconsin, 1101 University Avenue, Madison, Wisconsin 53706, United States.ORCID 0000-0003-4626-0863
Nathan M ShererMcArdle Laboratory for Cancer Research and Institute for Molecular Virology, University of Wisconsin, Madison, Wisconsin 53705, United States.
Lloyd M SmithDepartment of Chemistry, University of Wisconsin, 1101 University Avenue, Madison, Wisconsin 53706, United States.

Funding

Institutional Training in the Genomic SciencesT32HG002760 · NHGRI · UNIVERSITY OF WISCONSIN-MADISON · PI Qiongshi Lu · 2003 to 2026
$17.7M
The Center for HIV RNA Studies (CRNA)U54AI150470 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI TELESNITSKY, ALICE · 2019 to 2021
$15.1M
Chemistry-Biology Interface Training ProgramT32GM008505 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BLACKWELL, HELEN E. · 1993 to 2023
$9.8M
Revealing Proteoforms: The Primary Effectors of Biological FunctionR35GM126914 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI Lloyd M Smith · 2018 to 2026
$6.2M
The Cell Biology of HIV-1 Genome TraffickingR01AI110221 · NIAID · UNIVERSITY OF WISCONSIN-MADISON · PI Nathan M Sherer · 2014 to 2026
$4.4M
NHGRI NIH HHS T32 HG002760NIAID NIH HHS R01 AI110221NIAID NIH HHS U54 AI150470NIGMS NIH HHS R35 GM126914NIGMS NIH HHS T32 GM008505
6 · The paper itself

Abstract

Human immunodeficiency virus type 1 (HIV-1) remains a deadly infectious disease despite existing antiretroviral therapies. A comprehensive understanding of the specific mechanisms of viral infectivity remains elusive and currently limits the development of new and effective therapies. Through in-depth proteomic analysis of HIV-1 virions, we discovered the novel post-translational modification of highly conserved residues within the viral matrix and capsid proteins to the dehydroamino acids, dehydroalanine and dehydrobutyrine. We further confirmed their presence by labeling the reactive alkene, characteristic of dehydroamino acids, with glutathione via Michael addition. Dehydroamino acids are rare, understudied, and have been observed mainly in select bacterial and fungal species. Until now, they have not been observed in HIV proteins. We hypothesize that these residues are important in viral particle maturation and could provide valuable insight into HIV infectivity mechanisms.

Indexed as

HIV-1CapsidCapsid ProteinsHumansProteomicsVirionCapsid Proteinsbottom-up proteomicsdehydroalaninedehydrobutyrineHIV-1virion

Identifiers

PMID35192358
PMCPMC8976760

What OpenQuestion holds

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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.