Evidence map›Paper›PMID 23028850›Full record

ArticlePloS one2012

Inhibition of HIV-1 infection by human α-defensin-5, a natural antimicrobial peptide expressed in the genital and intestinal mucosae.

Lucinda Furci, Monica Tolazzi, Francesca Sironi, Lia Vassena, Paolo Lusso

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. 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
4.7field-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

19 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Peptide-Based Antiviral Drugs.Advances in experimental medicine and biology · 2021
    Article
  7. Antiviral Activities of Human Host Defense Peptides.Current medicinal chemistry · 2020
    Review
  8. Review
  9. Review
  10. Review
  11. The Role of Defensins in HIV Pathogenesis.Mediators of inflammation · 2017
    Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Antiviral mechanisms of human defensins.Journal of molecular biology · 2013
    Review
  18. Article
  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

5 authors at 2 institutions in 1 country.

Lucinda FurciUnit of Human Virology, Department of Biological and Technological Research, San Raffaele Scientific Institute, Milan, Italy. lucinda.furci@hsr.it
Monica Tolazzi
Francesca Sironi
Lia Vassena
Paolo Lusso
San Raffaele University of Rome · ITUniversity of Cagliari · IT

Funding

Role of IL-7 in Immune Defense against HIV-1 and Other Infectious PathogensZIAAI000976 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI LUSSO, PAOLO · 2009 to 2025
$9.1M
Natural Antiviral Factors Expressed by CD8+T Cells and Other Immune System CellsZIAAI001041 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI LUSSO, PAOLO · 2012 to 2017
$2.4M
6 · The paper itself

Abstract

backgroundα-defensin-5 (HD5) is a key effector of the innate immune system with broad anti-bacterial and anti-viral activities. Specialized epithelial cells secrete HD5 in the genital and gastrointestinal mucosae, two anatomical sites that are critically involved in HIV-1 transmission and pathogenesis. We previously found that human neutrophil defensins (HNP)-1 and -2 inhibit HIV-1 entry by specific bilateral interaction both with the viral envelope and with its primary cellular receptor, CD4. Despite low amino acid identity, human defensin-5 (HD5) shares with HNPs a high degree of structural homology. METHODOLOGY/PRINCIPAL

findingsHere, we demonstrate that HD5 inhibits HIV-1 infection of primary CD4(+) T lymphocytes at low micromolar concentration under serum-free and low-ionic-strength conditions similar to those occurring in mucosal fluids. Blockade of HIV-1 infection was observed with both primary and laboratory-adapted strains and was independent of the viral coreceptor-usage phenotype. Similar to HNPs, HD5 inhibits HIV-1 entry into the target cell by interfering with the reciprocal interaction between the external envelope glycoprotein, gp120, and CD4. At high concentrations, HD5 was also found to downmodulate expression of the CXCR4 coreceptor, but not of CCR5. Consistent with its broad spectrum of activity, antibody competition studies showed that HD5 binds to a region overlapping with the CD4- and coreceptor-binding sites of gp120, but not to the V3 loop region, which contains the major determinants of coreceptor-usage specificity. CONCLUSION/SIGNIFICANCE: These findings provide new insights into the first line of immune defense against HIV-1 at the mucosal level and open new perspectives for the development of preventive and therapeutic strategies.

Indexed as

alpha-DefensinsCCR5 Receptor AntagonistsCD4-Positive T-LymphocytesCells, CulturedFemaleGene ExpressionGenitaliaHIV-1HIV Envelope Protein gp120HIV InfectionsHumansIntestinal MucosaMaleMucous MembraneReceptors, CCR5Receptors, CXCR4alpha-DefensinsCCR5 Receptor AntagonistsDEFA5 protein, humanHIV Envelope Protein gp120human neutrophil peptide 1human neutrophil peptide 2Receptors, CCR5Receptors, CXCR4Recombinant Proteins

Identifiers

PMID23028850
PMCPMC3459904
OpenAlexW2063456659

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.