Evidence map›Paper›PMID 35019698›Full record

ArticleMicrobiology spectrum2022

MARCH8 Targets Cytoplasmic Lysine Residues of Various Viral Envelope Glycoproteins.

Yanzhao Zhang, Seiya Ozono, Takuya Tada, Minoru Tobiume, Masanori Kameoka, Satoshi Kishigami, Hideaki Fujita, Kenzo Tokunaga

Open access · goldAbstract read
In one paragraph

Article in Microbiology spectrum, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
7.3field-weighted citation impact, top 2% 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

23 citing papers in PubMed, 31 citations in OpenAlex.

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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

8 authors at 4 institutions in 2 countries.

Yanzhao ZhangDepartment of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.ORCID 0000-0002-1937-4438
Seiya OzonoDepartment of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.ORCID 0000-0002-1764-2937
Takuya TadaDepartment of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.ORCID 0000-0003-0779-9954
Minoru TobiumeDepartment of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.ORCID 0000-0001-9110-2915
Masanori KameokaDepartment of Public Health, Kobe University Graduate School of Health Sciences, Hyogo, Japan.ORCID 0000-0001-5525-9915
Satoshi KishigamiFaculty of Life and Environmental Sciences, University of Yamanashi, Yamanashi, Japan.ORCID 0000-0001-9447-5100
Hideaki FujitaFaculty of Pharmaceutical Sciences, Nagasaki International University, Nagasaki, Japan.ORCID 0000-0002-4105-4430
Kenzo TokunagaDepartment of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.ORCID 0000-0002-2625-5322
National Institute of Infectious Diseases · JPHyogo University of Health Sciences · JPNagasaki International University · JPUniversity of Yamanashi · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The host transmembrane protein MARCH8 is a RING finger E3 ubiquitin ligase that downregulates various host transmembrane proteins, such as MHC-II. We have recently reported that MARCH8 expression in virus-producing cells impairs viral infectivity by reducing virion incorporation of not only HIV-1 envelope glycoprotein but also vesicular stomatitis virus G-glycoprotein through two different pathways. However, the MARCH8 inhibition spectrum remains largely unknown. Here, we show the antiviral spectrum of MARCH8 using viruses pseudotyped with a variety of viral envelope glycoproteins. Infection experiments revealed that viral envelope glycoproteins derived from the rhabdovirus, arenavirus, coronavirus, and togavirus (alphavirus) families were sensitive to MARCH8-mediated inhibition. Lysine mutations at the cytoplasmic tails of rabies virus-G, lymphocytic choriomeningitis virus glycoproteins, SARS-CoV and SARS-CoV-2 spike proteins, and Chikungunya virus and Ross River virus E2 proteins conferred resistance to MARCH8. Immunofluorescence showed impaired downregulation of the mutants of these viral envelope glycoproteins by MARCH8, followed by lysosomal degradation, suggesting that MARCH8-mediated ubiquitination leads to intracellular degradation of these envelopes. Indeed, rabies virus-G and Chikungunya virus E2 proteins proved to be clearly ubiquitinated. We conclude that MARCH8 has inhibitory activity on a variety of viral envelope glycoproteins whose cytoplasmic lysine residues are targeted by this antiviral factor.

Indexed as

Antiviral AgentsBlotting, WesternDown-RegulationHEK293 CellsHeLa CellsHumansImmunoprecipitationLysineUbiquitinationUbiquitin-Protein LigasesViral Envelope ProteinsAntiviral AgentsLysineMARCHF8 protein, humanUbiquitin-Protein LigasesViral Envelope ProteinsdegradationdownregulationMARCH8ubiquitinationviral envelope glycoprotein

Identifiers

PMID35019698
PMCPMC8754143
OpenAlexW4220937769

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.