Evidence map›Paper›PMID 15367629›Full record

ArticleJournal of virology2004

Profile of resistance of human immunodeficiency virus to mannose-specific plant lectins.

Jan Balzarini, Kristel Van Laethem, Sigrid Hatse, Kurt Vermeire, Erik De Clercq, Willy Peumans, Els Van Damme, Anne-Mieke Vandamme, Anders Bölmstedt, Dominique Schols and 1 more

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

43 citing papers in PubMed, 102 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. HIV-1 gp120 as a therapeutic target: navigating a moving labyrinth.Expert opinion on therapeutic targets · 2015
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Molecular architecture and therapeutic potential of lectin mimics.Advances in carbohydrate chemistry and biochemistry · 2012
    Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
    Böhlmstedt, Anders [corrected to Bölmstedt, Anders]
5 · Who and what money

Authors and funding

11 authors at 2 institutions in 2 countries.

Jan BalzariniRega Institute for Medical Research, Gent, Belgium. jan.balzarini@rega.kuleuven.ac.be
Kristel Van Laethem
Sigrid Hatse
Kurt Vermeire
Erik De Clercq
Willy Peumans
Els Van Damme
Anne-Mieke Vandamme
Anders Bölmstedt
Dominique Schols
Anders Böhlmstedt
Rega Institute for Medical Research · BESwedish Institute · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mannose-specific plant lectins from the Amaryllidaceae family (e.g., Hippeastrum sp. hybrid and Galanthus nivalis) inhibit human immunodeficiency virus (HIV) infection of human lymphocytic cells in the higher nanogram per milliliter range and suppress syncytium formation between persistently HIV type 1 (HIV-1)-infected cells and uninfected CD4(+) T cells. These lectins inhibit virus entry. When exposed to escalating concentrations of G. nivalis and Hippeastrum sp. hybrid agglutinin, a variety of HIV-1(III(B)) strains were isolated after 20 to 40 subcultivations which showed a decreased sensitivity to the plant lectins. Several amino acid changes in the envelope glycoprotein gp120, but not in gp41, of the mutant virus isolates were observed. The vast majority of the amino acid changes occurred at the N glycosylation sites and at the S or T residues that are part of the N glycosylation motif. The degree of resistance to the plant lectins was invariably correlated with an increasing number of mutated glycosylation sites in gp120. The nature of these mutations was entirely different from that of mutations that are known to appear in HIV-1 gp120 under the pressure of other viral entry inhibitors such as dextran sulfate, bicyclams (i.e., AMD3100), and chicoric acid, which also explains the lack of cross-resistance of plant lectin-resistant viruses to any other HIV inhibitor including T-20 and the blue-green algae (cyanobacteria)-derived mannose-specific cyanovirin. The plant lectins represent a well-defined class of anti-HIV (microbicidal) drugs with a novel HIV drug resistance profile different from those of other existing anti-HIV drugs.

Indexed as

Amino Acid SubstitutionAnti-HIV AgentsBacterial ProteinsBenzylaminesCaffeic AcidsCarrier ProteinsCell LineCoculture TechniquesCyclamsDextran SulfateDrug Resistance, ViralEnfuvirtideGiant CellsGlycosylationHeterocyclic CompoundsHIVAnti-HIV AgentsBacterial ProteinsBenzylaminesCaffeic AcidsCarrier Proteinschicoric acidcyanovirin NCyclamsDextran SulfateEnfuvirtideHeterocyclic CompoundsHIV Envelope Protein gp120HIV Envelope Protein gp41Peptide FragmentsPlant LectinsplerixaforReceptors, HIVSuccinates

Identifiers

PMID15367629
PMCPMC516383
OpenAlexW2124141618

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.