Evidence map›Paper›PMID 26523972›Full record

ArticleNature medicine2015

MARCH8 inhibits HIV-1 infection by reducing virion incorporation of envelope glycoproteins.

Takuya Tada, Yanzhao Zhang, Takayoshi Koyama, Minoru Tobiume, Yasuko Tsunetsugu-Yokota, Shoji Yamaoka, Hideaki Fujita, Kenzo Tokunaga

Abstract read
PubMed Publisher
In one paragraph

Article in Nature medicine, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed, 1 pooled it
4.6field-weighted citation impact, top 5% 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

96 citing papers in PubMed, 1 synthesis or guideline pooled it, 145 citations in OpenAlex.

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36 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Takuya TadaDepartment of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.
Yanzhao ZhangDepartment of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.
Takayoshi KoyamaDepartment of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.
Minoru TobiumeDepartment of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.
Yasuko Tsunetsugu-YokotaDepartment of Immunology, National Institute of Infectious Diseases, Tokyo, Japan.ORCID http://orcid.org/0000-0002-1168-8846
Shoji YamaokaDepartment of Molecular Virology, Tokyo Medical and Dental University, Tokyo, Japan.
Hideaki FujitaFaculty of Pharmaceutical Sciences, Nagasaki International University, Nagasaki, Japan.
Kenzo TokunagaDepartment of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.
National Institute of Infectious Diseases · JPTokyo Medical and Dental University · JPNagasaki International University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane-associated RING-CH 8 (MARCH8) is one of 11 members of the recently discovered MARCH family of RING (really interesting new gene)-finger E3 ubiquitin ligases. MARCH8 downregulates several host transmembrane proteins, including major histocompatibility complex (MHC)-II, CD86, interleukin (IL)-1 receptor accessory protein, TNF-related apoptosis-inducing ligand (TRAIL) receptor 1 and the transferrin receptor. However, its physiological roles remain largely unknown. Here we identify MARCH8 as a novel antiviral factor. The ectopic expression of MARCH8 in virus-producing cells does not affect levels of lentivirus production, but it does markedly reduce viral infectivity. MARCH8 blocks the incorporation of HIV-1 envelope glycoprotein into virus particles by downregulating it from the cell surface, probably through their interaction, resulting in a substantial reduction in the efficiency of viral entry. The inhibitory effect of MARCH8 on vesicular stomatitis virus G-glycoprotein is even more remarkable, suggesting a broad-spectrum inhibition of enveloped viruses by MARCH8. Notably, the endogenous expression of MARCH8 is high in monocyte-derived macrophages and dendritic cells, and MARCH8 knockdown or knockout in macrophages significantly increases the infectivity of virions produced by these cells. Our findings thus indicate that MARCH8 is highly expressed in terminally differentiated myeloid cells, and that it is a potent antiviral protein that targets viral envelope glycoproteins and reduces their incorporation into virions.

Indexed as

Cell MembraneDown-Regulationenv Gene Products, Human Immunodeficiency VirusGene SilencingHEK293 CellsHIV-1HIV InfectionsHumansLentivirusMacrophagesMembrane GlycoproteinsProtein BindingProtein Structure, TertiaryRNA, MessengerTransduction, GeneticUbiquitin-Protein Ligasesenv Gene Products, Human Immunodeficiency VirusG protein, vesicular stomatitis virusMARCHF8 protein, humanMembrane GlycoproteinsRNA, MessengerUbiquitin-Protein LigasesViral Envelope Proteins

Identifiers

PMID26523972
OpenAlexW1931451499

What OpenQuestion holds

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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.