Evidence map›Paper›PMID 42031325›Full record

ArticleJournal of molecular biology2026

Identification of Non-basic Matrix Domain Residues That Impact HTLV-1 Gag Membrane Targeting and Particle Release.

Shuyu Meng, Bao Pham, Sophie Hines, Isaac Angert, Dalton W Piotter, Joachim D Mueller, Jamil S Saad, Wei Zhang, Louis M Mansky

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of molecular biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

9 authors.

Shuyu MengMolecular Pharmacology and Therapeutics Graduate Program, University of Minnesota - Twin Cities, Minneapolis, MN 55455, USA; Institute for Molecular Virology, University of Minnesota - Twin Cities, Minneapolis, MN 55455, USA; Masonic Cancer Center, University of Minnesota - Twin Cities, Minneapolis, MN 55455, USA.
Bao PhamDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294.
Sophie HinesDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294.
Isaac AngertInstitute for Molecular Virology, University of Minnesota - Twin Cities, Minneapolis, MN 55455, USA; School of Astronomy and Physics, University of Minnesota - Twin Cities, Minneapolis, MN 55455, USA.
Dalton W PiotterInstitute for Molecular Virology, University of Minnesota - Twin Cities, Minneapolis, MN 55455, USA; Masonic Cancer Center, University of Minnesota - Twin Cities, Minneapolis, MN 55455, USA; Biochemistry, Molecular Biology, and Biophysics Graduate Program, University of Minnesota - Twin Cities, Minneapolis, MN 55455, USA.
Joachim D MuellerInstitute for Molecular Virology, University of Minnesota - Twin Cities, Minneapolis, MN 55455, USA; Masonic Cancer Center, University of Minnesota - Twin Cities, Minneapolis, MN 55455, USA; School of Astronomy and Physics, University of Minnesota - Twin Cities, Minneapolis, MN 55455, USA.
Jamil S SaadDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294.
Wei ZhangInstitute for Molecular Virology, University of Minnesota - Twin Cities, Minneapolis, MN 55455, USA; Department of Diagnostic & Biological Sciences, School of Dentistry, University of Minnesota - Twin Cities, Minneapolis, MN 55455, USA; Masonic Cancer Center, University of Minnesota - Twin Cities, Minneapolis, MN 55455, USA; Characterization Facility, University of Minnesota - Twin Cities, Minneapolis, MN 55455, USA.
Louis M ManskyMolecular Pharmacology and Therapeutics Graduate Program, University of Minnesota - Twin Cities, Minneapolis, MN 55455, USA; Institute for Molecular Virology, University of Minnesota - Twin Cities, Minneapolis, MN 55455, USA; Department of Diagnostic & Biological Sciences, School of Dentistry, University of Minnesota - Twin Cities, Minneapolis, MN 55455, USA; Masonic Cancer Center, University of Minnesota - Twin Cities, Minneapolis, MN 55455, USA; Biochemistry, Molecular Biology, and Biophysics Graduate Program, University of Minnesota - Twin Cities, Minneapolis, MN 55455, USA. Electronic address: mansky@umn.edu.

Funding

XRAY CRYSTALLOGRAPHYP30CA013148 · NCI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI Omer Jamy · 1985 to 2026
$165.9M
TRD3 NMRbox: Bayesian AnalyticsP41GM111135 · NIGMS · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI HOCH, JEFFREY C · 2015 to 2024
$14.0M
Structural basis for HIV-1 Gag interactions with cellular and viral constituentsR01AI150901 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI Terje Dokland · 2019 to 2026
$2.9M
Deltaretrovirus Morphology and Particle AssemblyR01GM151775 · NIGMS · UNIVERSITY OF MINNESOTA · PI JOACHIM D MUELLER, Louis M Mansky · 2024 to 2026
$1.7M
Structural Basis for HIV-1 Gag assembly and Env incorporationR37AI150901 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI SAAD, JAMIL SUBHI · 2023 to 2024
$1.2M
Imaging of HTLV-1 by cryo-CLEMR21DE032878 · NIDCR · UNIVERSITY OF MINNESOTA · PI MANSKY, LOUIS M. · 2023 to 2024
$595k
NCI NIH HHS P30 CA013148NIAID NIH HHS R01 AI150901NIAID NIH HHS R37 AI150901NIDCR NIH HHS R21 DE032878NIGMS NIH HHS P41 GM111135NIGMS NIH HHS R01 GM151775
6 · The paper itself

Abstract

The matrix (MA) domain of the Gag polyprotein is critical for directing retroviral assembly at the plasma membrane (PM), yet the determinants mediating human T-cell leukemia virus type 1 (HTLV-1) Gag targeting remain incompletely defined. While Gag myristoylation and basic residue-mediated electrostatic interactions are known to be crucial for Gag-PM interactions, recent evidence with HTLV-1 MA has implicated limited dependence on specific lipid headgroup recognition for Gag interaction with the PM. Here, we have analyzed the role of non-basic residues in HTLV-1 MA in membrane interactions and particle assembly. We identified several residues (i.e., L19, D42, S70, and L71) that were essential for Gag targeting to the PM, where mutation of these amino acid residues led to Gag targeting to internal locations that colocalized with late endosomal markers. Mutation of L19 and D42 was found to alter the MA structure. Taken together, these data indicate that mutation of MA non-basic amino acid residues affected particle production and also led to Gag localization to internal membranes that colocalized with late endosomal markers. These observations indicate that non-basic residues play an important role in efficient particle assembly and release of HTLV-1 from cells.

Indexed as

Cell MembraneGene Products, gagHuman T-lymphotropic virus 1Virus ReleaseHumansMutationProtein DomainsVirionVirus AssemblyGene Products, gagGag polyproteinhuman immunodeficiency virus type 1human T-cell leukemia virus type 1matrix protein domainplasma membrane

Identifiers

PMID42031325
PMCPMC13180280

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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.