Evidence map›Paper›PMID 39264155›Full record

ArticleJournal of virology2024

Characterization of bi-segmented and tri-segmented recombinant Pichinde virus particles.

Hannah Murphy, Qinfeng Huang, Jacob Jensen, Noah Weber, Luiza Mendonça, Hinh Ly, Yuying Liang

Abstract read
In one paragraph

Article in Journal of virology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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.

Hannah MurphyDepartment of Veterinary and Biomedical Sciences, College of Veterinary Medicine, University of Minnesota, St. Paul, Minnesota, USA.ORCID 0000-0001-5958-8345
Qinfeng HuangDepartment of Veterinary and Biomedical Sciences, College of Veterinary Medicine, University of Minnesota, St. Paul, Minnesota, USA.
Jacob JensenDepartment of Biochemistry, Molecular Biology and Biophysics, College of Biological Sciences, University of Minnesota, Twin Cities, Minneapolis, Minnesota, USA.
Noah WeberDepartment of Biochemistry, Molecular Biology and Biophysics, College of Biological Sciences, University of Minnesota, Twin Cities, Minneapolis, Minnesota, USA.
Luiza MendonçaDepartment of Biochemistry, Molecular Biology and Biophysics, College of Biological Sciences, University of Minnesota, Twin Cities, Minneapolis, Minnesota, USA.
Hinh LyDepartment of Veterinary and Biomedical Sciences, College of Veterinary Medicine, University of Minnesota, St. Paul, Minnesota, USA.ORCID 0000-0001-8271-2033
Yuying LiangDepartment of Veterinary and Biomedical Sciences, College of Veterinary Medicine, University of Minnesota, St. Paul, Minnesota, USA.ORCID 0000-0001-6002-6868

Funding

Mechanism of Lassa fever virus Z protein in immune suppression and viral virulenceR01AI131586 · NIAID · UNIVERSITY OF MINNESOTA · PI LIANG, YUYING, LY, HINH · 2017 to 2021
$3.8M
Minnesota Training Program in VirologyT32AI083196 · NIAID · UNIVERSITY OF MINNESOTA · PI Louis M Mansky · 2010 to 2026
$3.2M
A transformative next-generation Orbitrap Tribrid system for the UMN and Upper MidwestS10OD028717 · OD · UNIVERSITY OF MINNESOTA · PI GRIFFIN, TIMOTHY J. · 2020 to 2020
$1.2M
NIAID NIH HHS R01 AI131586NIAID NIH HHS T32 AI083196NIH HHS S10 OD028717
6 · The paper itself

Abstract

Mammarenaviruses include several highly virulent pathogens (e.g., Lassa virus) capable of causing severe hemorrhagic fever diseases for which there are no approved vaccines and limited treatment options. Mammarenaviruses are enveloped, bi-segmented ambisense RNA viruses. There is limited knowledge about cellular proteins incorporated into progeny virion particles and their potential biological roles in viral infection. Pichinde virus (PICV) is a prototypic arenavirus used to characterize mammarenavirus replication and pathogenesis. We have developed a recombinant PICV with a tri-segmented RNA genome as a viral vector platform. Whether the tri-segmented virion differs from the wild-type bi-segmented one in viral particle morphology and protein composition has not been addressed. In this study, recombinant PICV (rPICV) virions with a bi-segmented (rP18bi) and a tri-segmented (rP18tri) genome were purified by density-gradient ultracentrifugation and analyzed by cryo-electron microscopy and mass spectrometry. Both virion types are pleomorphic with spherical morphology and have no significant difference in size despite rP18tri having denser particles. Both virion types also contain similar sets of cellular proteins. Among the highly enriched virion-associated cellular proteins are components of the endosomal sorting complex required for transport pathway and vesicle trafficking, such as ALIX, Tsg101, VPS, CHMP, and Ras-associated binding proteins, which have known functions in virus assembly and budding. Other enriched cellular proteins include peripheral and transmembrane proteins, chaperone proteins, and ribosomal proteins; their biological roles in viral infection warrant further analysis. Our study provides important insights into mammarenavirus particle formation and aids in the future development of viral vectors and antiviral discovery.IMPORTANCEMammarenaviruses, such as Lassa virus, are enveloped RNA viruses that can cause severe hemorrhagic fever diseases (Lassa fever) with no approved vaccine and limited therapeutic options. Cellular proteins incorporated into progeny virion particles and their biological roles in mammarenavirus infection have not been well characterized. Pichinde virus (PICV) is a prototypic mammarenavirus used as a surrogate model for Lassa fever. We used cryo-electron microscopy and proteomic analysis to characterize the morphology and protein contents of the purified PICV particles that package either two (bi-segmented) or three (tri-segmented) genomic RNA segments. Our results demonstrate a similar virion morphology but different particle density for the bi- and tri-segmented viral particles and reveal major virion-associated cellular proteins. This study provides important insights into the virus-host interactions that can be used for antiviral development and optimizing arenavirus-based vaccine vectors.

Indexed as

Cryoelectron MicroscopyGenome, ViralPichinde virusVirionAnimalsChlorocebus aethiopsHumansLassa virusRNA, ViralVero CellsViral ProteinsVirus AssemblyVirus ReplicationRNA, ViralViral Proteinsarenaviruscryoelectron microscopycryotomographymass spectrometryPichinde virusvirion-associated proteinsvirion structure

Identifiers

PMID39264155
PMCPMC11494906

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.