Evidence map›Paper›PMID 17229699›Full record

ArticleJournal of virology2007

Immunoglobulin A (IgA) is a natural ligand of hepatitis A virus cellular receptor 1 (HAVCR1), and the association of IgA with HAVCR1 enhances virus-receptor interactions.

Cecilia Tami, Erica Silberstein, Mohanraj Manangeeswaran, Gordon J Freeman, Sarah E Umetsu, Rosemarie H DeKruyff, Dale T Umetsu, Gerardo G Kaplan

Abstract read
In one paragraph

Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed, 1 pooled it
2.2field-weighted citation impact, top 11% 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

22 citing papers in PubMed, 1 synthesis or guideline pooled it, 60 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Review
  4. Review
  5. Role of TIM-1 in the development and treatment of tumours.Frontiers in cell and developmental biology · 2024
    Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Costimulatory pathways in transplantation.Seminars in immunology · 2011
    Article
  15. Article
  16. Review
  17. Article
  18. Picornaviruses.Current topics in microbiology and immunology · 2010
    Article
  19. The costimulatory role of TIM molecules.Immunological reviews · 2009
    Review
  20. 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

8 authors at 4 institutions in 1 country.

Cecilia TamiLaboratory of Hepatitis and Related Emerging Agents, CBER, Food and Drug Administration, Bethesda, MD 20892, USA.
Erica Silberstein
Mohanraj Manangeeswaran
Gordon J Freeman
Sarah E Umetsu
Rosemarie H DeKruyff
Dale T Umetsu
Gerardo G Kaplan
United States Food and Drug Administration · USBoston Children's Hospital · USDana-Farber Cancer Institute · USNorthwestern University · US

Funding

TIM recognition of phosphatidylserine regulates innate and adaptive immunityP01AI054456 · NIAID · STANFORD UNIVERSITY · PI FREEMAN, GORDON JAMES · 2003 to 2014
$12.8M
NIAID NIH HHS P01 AI054456NIAID NIH HHS P01 AI 54456
6 · The paper itself

Abstract

The hepatitis A virus cellular receptor 1 (HAVCR1/TIM1), a member of the T-cell immunoglobulin mucin (TIM) family, is an important atopy susceptibility gene in humans. The exact natural function of HAVCR1/TIM1 and the inverse association between HAV infection and prevention of atopy are not well understood. To identify natural ligands of human HAVCR1/TIM1, we used an expression cloning strategy based on the binding of dog cells transfected with a human lymph node cDNA library to a HAVCR1/TIM1 Fc fusion protein. The transfected cells that bound to the human HAVCR1/TIM1 Fc contained cDNA of human immunoglobulin alpha 1 heavy (Igalpha1) and lambda light (Iglambda) chain and secreted human IgA1lambda antibody that bound to the cell surface. Cotransfection of the isolated Igalpha1 and Iglambda cDNAs to naïve dog cells resulted in the secretion of IgA1lambda that bound to HAVCR1/TIM1 Fc but not to a poliovirus receptor Fc fusion protein in a capture enzyme-linked immunosorbent assay. The interaction of HAVCR1/TIM1 with IgA was inhibited by monoclonal antibodies (MAbs) against Igalpha1 and Iglambda, excess IgA1lambda, or anti-HAVCR1/TIM1 MAb. IgA did not inhibit HAV infection of African green monkey cells, suggesting that the IgA and the virus binding sites are in different epitopes on HAVCR1/TIM1. IgA enhanced significantly the neutralization of HAV by HAVCR1/TIM1 Fc. Our results indicate that IgA1lambda is a specific ligand of HAVCR1/TIM1 and that their association has a synergistic effect in virus-receptor interactions.

Indexed as

Virus InternalizationAnimalsCell LineCell MembraneChlorocebus aethiopsCloning, MolecularCricetinaeGene ExpressionHepatitis A virusHepatitis A Virus Cellular Receptor 1HumansImmunoglobulin ALigandsMembrane GlycoproteinsProtein BindingReceptors, VirusHAVCR1 protein, humanHepatitis A Virus Cellular Receptor 1Immunoglobulin ALigandsMembrane GlycoproteinsReceptors, Virus

Identifiers

PMID17229699
PMCPMC1866050
OpenAlexW2171242275

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.