Evidence map›Paper›PMID 27655726›Full record

ArticleOncotarget2016

Gamma-interferon-inducible, lysosome/endosome-localized thiolreductase, GILT, has anti-retroviral activity and its expression is counteracted by HIV-1.

Yoshinao Kubo, Mai Izumida, Yuka Yashima, Haruka Yoshii-Kamiyama, Yuetsu Tanaka, Kiyoshi Yasui, Hideki Hayashi, Toshifumi Matsuyama

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed, 1 pooled it
1.6field-weighted citation impact, top 16% 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

13 citing papers in PubMed, 1 synthesis or guideline pooled it, 20 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 2 institutions in 2 countries.

Yoshinao KuboDivision of Cytokine Signaling, Graduate School of Medical Sciences, Nagasaki University, Nagasaki, Japan.
Mai IzumidaDivision of Cytokine Signaling, Graduate School of Medical Sciences, Nagasaki University, Nagasaki, Japan.
Yuka YashimaDivision of Cytokine Signaling, Graduate School of Medical Sciences, Nagasaki University, Nagasaki, Japan.
Haruka Yoshii-KamiyamaDivision of Cytokine Signaling, Graduate School of Medical Sciences, Nagasaki University, Nagasaki, Japan.
Yuetsu TanakaDepartment of Immunology, Graduate School and Faculty of Medicine, University of the Ryukyus, Okinawa, Japan.
Kiyoshi YasuiDivision of Cytokine Signaling, Graduate School of Medical Sciences, Nagasaki University, Nagasaki, Japan.
Hideki HayashiDivision of Cytokine Signaling, Graduate School of Medical Sciences, Nagasaki University, Nagasaki, Japan.
Toshifumi MatsuyamaDivision of Cytokine Signaling, Graduate School of Medical Sciences, Nagasaki University, Nagasaki, Japan.
Nagasaki University · JPHarvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanism by which type II interferon (IFN) inhibits virus replications remains to be identified. Murine leukemia virus (MLV) replication was significantly restricted by γ-IFN, but not human immunodeficiency virus type 1 (HIV-1) replication. Because MLV enters host cells via endosomes, we speculated that certain cellular factors among γ-IFN-induced, endosome-localized proteins inhibit MLV replication. We found that γ-IFN-inducible lysosomal thiolreductase (GILT) significantly restricts HIV-1 replication as well as MLV replication by its thiolreductase activity. GILT silencing enhanced replication-defective HIV-1 vector infection and virion production in γ-IFN-treated cells, although γ-IFN did not inhibit HIV-1 replication. This result showed that GILT is required for the anti-viral activity of γ-IFN. Interestingly, GILT protein level was increased by γ-IFN in uninfected cells and env-deleted HIV-1-infected cells, but not in full-length HIV-1-infected cells. γ-IFN-induced transcription from the γ-IFN-activation sequence was attenuated by the HIV-1 Env protein. These results suggested that the γ-IFN cannot restrict HIV-1 replication due to the inhibition of γ-IFN signaling by HIV-1 Env. Finally, we found that 4,4'-dithiodipyridine (4-PDS), which inhibits S-S bond formation at acidic pH, significantly suppresses HIV-1 vector infection and virion production, like GILT. In conclusion, this study showed that GILT functions as a host restriction factor against the retroviruses, and a GILT mimic, 4-PDS, is the leading compound for the development of novel concept of anti-viral agents.

Indexed as

AnimalsAnti-Retroviral AgentsChlorocebus aethiopsCOS CellsDithionitrobenzoic AcidGene Products, envHIV-1HumansInterferon-gammaLeukemia Virus, MurineMiceOxidoreductases Acting on Sulfur Group DonorsTetraspanin 30VirionVirus ReplicationAnti-Retroviral AgentsDithionitrobenzoic AcidGene Products, envIFI30 protein, humanInterferon-gammaOxidoreductases Acting on Sulfur Group DonorsTetraspanin 30antiviralendosomegamma-interferonretrovirusesthiolreductase

Identifiers

PMID27655726
PMCPMC5342076
OpenAlexW2520302623

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.