Evidence map›Paper›PMID 17989173›Full record

ArticleJournal of virology2008

Modulation of human immunodeficiency virus type 1 infectivity through incorporation of tetraspanin proteins.

Kei Sato, Jun Aoki, Naoko Misawa, Eriko Daikoku, Kouichi Sano, Yuetsu Tanaka, Yoshio Koyanagi

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed, 1 pooled it
3.0field-weighted citation impact, top 8% 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

81 citing papers in PubMed, 1 synthesis or guideline pooled it, 120 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Exosomal transmission of viruses, a two-edged biological sword.Cell communication and signaling : CCS · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Tetraspanins: Host Factors in Viral Infections.International journal of molecular sciences · 2021
    Review
  13. Review
  14. Review
  15. Article
  16. Tetraspanins in the regulation of mast cell function.Medical microbiology and immunology · 2020
    Review
  17. Review
  18. Review
  19. Article
  20. Review

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

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 at 3 institutions in 1 country.

Kei SatoLaboratory of Viral Pathogenesis, Institute for Virus Research, Kyoto University, 53 Shogoinkawara-cho, Sakyo-ku, Kyoto, Kyoto 606-8507, Japan.
Jun Aoki
Naoko Misawa
Eriko Daikoku
Kouichi Sano
Yuetsu Tanaka
Yoshio Koyanagi
Kyoto University · JPOsaka Medical and Pharmaceutical University · JPUniversity of the Ryukyus · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Accumulating evidence indicates that human immunodeficiency virus type 1 (HIV-1) acquires various cellular membrane proteins in the lipid bilayer of the viral envelope membrane. Although some virion-incorporated cellular membrane proteins are known to potently affect HIV-1 infectivity, the virological functions of most virion-incorporated membrane proteins remain unclear. Among these host proteins, we found that CD63 was eliminated from the plasma membranes of HIV-1-producing T cells after activation, followed by a decrease in the amount of virion-incorporated CD63, and in contrast, an increase in the infectivity of the released virions. On the other hand, we found that CD63 at the cell surface was preferentially embedded on the membrane of released virions in an HIV-1 envelope protein (Env)-independent manner and that virion-incorporated CD63 had the potential to inhibit HIV-1 Env-mediated infection in a strain-specific manner at the postattachment entry step(s). In addition, these behaviors were commonly observed in other tetraspanin proteins, such as CD9, CD81, CD82, and CD231. However, L6 protein, whose topology is similar to that of tetraspanins but which does not belong to the tetraspanin superfamily, did not have the potential to prevent HIV-1 infection, despite its successful incorporation into the released particles. Taken together, these results suggest that tetraspanin proteins have the unique potential to modulate HIV-1 infectivity through incorporation into released HIV-1 particles, and our findings may provide a clue to undiscovered aspects of HIV-1 entry.

Indexed as

Virus InternalizationAntigens, CDAntigens, SurfaceCell LineHIV-1HumansKangai-1 ProteinMembrane GlycoproteinsMembrane ProteinsNeoplasm ProteinsNerve Tissue ProteinsPlatelet Membrane GlycoproteinsTetraspanin 28Tetraspanin 29Tetraspanin 30TetraspaninsAntigens, CDAntigens, SurfaceCD63 protein, humanCD81 protein, humanCD82 protein, humanCD9 protein, humanKangai-1 ProteinMembrane GlycoproteinsMembrane ProteinsNeoplasm ProteinsNerve Tissue ProteinsPlatelet Membrane GlycoproteinsTetraspanin 28Tetraspanin 29Tetraspanin 30TetraspaninsTM4SF1 protein, humanTSPAN7 protein, human

Identifiers

PMID17989173
PMCPMC2224585
OpenAlexW2002381405

What OpenQuestion holds

Textmetadata
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.