Evidence map›Paper›PMID 32796070›Full record

ArticleJournal of virology2020

SERINC5 Inhibits HIV-1 Infectivity by Altering the Conformation of gp120 on HIV-1 Particles.

Austin Featherstone, Christopher Aiken

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

19 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. SERINC5 counters retroviruses and non-retroviruses.Frontiers in cellular and infection microbiology · 2024
    Review
  8. Article
  9. Article
  10. HIV-1 restriction by SERINC5.Medical microbiology and immunology · 2023
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. 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

2 authors at 1 institution in 1 country.

Austin FeatherstoneVanderbilt University Medical Center, Department of Pathology, Microbiology and Immunology, Nashville, Tennessee, USA.
Christopher AikenVanderbilt University Medical Center, Department of Pathology, Microbiology and Immunology, Nashville, Tennessee, USA chris.aiken@vumc.org.ORCID 0000-0002-2476-4078
Vanderbilt University Medical Center · US

Funding

X-Ray Core P50GM082251 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ENGELMAN, ALAN N. · 2007 to 2018
$48.1M
Technology Development 2: MAS NMR and dynamic nuclear polarization for HIV-1 structural biologyP50AI150481 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI GRONENBORN, ANGELA M. · 2019 to 2021
$14.1M
MOLECULAR PARASITOLOGY TRAINING PROGRAMT32AI007281 · NIAID · MEHARRY MEDICAL COLLEGE · PI NDE, PIUS N · 1985 to 2025
$3.2M
NIAID NIH HHS P50 AI150481NIAID NIH HHS T32 AI007281NIGMS NIH HHS P50 GM082251
6 · The paper itself

Abstract

SERINC5 is a 10-transmembrane-domain cellular protein that is incorporated into budding HIV-1 particles and reduces HIV-1 infectivity by inhibiting virus-cell fusion. HIV-1 susceptibility to SERINC5 is determined by sequences in the viral Env glycoprotein gp120, and the antiviral effect of SERINC5 is counteracted by the viral accessory protein Nef. While the precise mechanism by which SERINC5 inhibits HIV-1 infectivity is unclear, previous studies have suggested that SERINC5 affects Env conformation. To define the effects of SERINC5 on Env conformation, we quantified the binding of HIV-1 particles to immobilized Env-specific monoclonal antibodies. We observed that SERINC5 reduced the binding of HIV-1 particles bearing a SERINC5-susceptible Env to antibodies that recognize the V3 loop, a soluble CD4 (sCD4)-induced epitope, and an N-linked glycan. In contrast, SERINC5 did not alter the capture of HIV-1 particles bearing the SERINC5-resistant Env protein. Moreover, the effect of SERINC5 on antibody-dependent virus capture was abrogated by Nef expression. Our results indicate that SERINC5 inhibits HIV-1 infectivity by altering the conformation of gp120 on virions and/or physical masking of specific HIV-1 Env epitopes.

Indexed as

CD4 AntigensHEK293 CellsHIV-1HIV Envelope Protein gp120HIV InfectionsHumansMembrane ProteinsProtein Structure, SecondaryCD4 Antigensgp120 protein, Human immunodeficiency virus 1HIV Envelope Protein gp120Membrane ProteinsSERINC5 protein, humanantiviral mechanismgp120HIV-1host defensesNefrestriction factorSERINC5

Identifiers

PMID32796070
PMCPMC7527050
OpenAlexW3048633356

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.