Evidence map›Paper›PMID 17050611›Full record

ArticleJournal of virology2007

Pradimicin A, a carbohydrate-binding nonpeptidic lead compound for treatment of infections with viruses with highly glycosylated envelopes, such as human immunodeficiency virus.

Jan Balzarini, Kristel Van Laethem, Dirk Daelemans, Sigrid Hatse, Antonella Bugatti, Marco Rusnati, Yasuhiro Igarashi, Toshikazu Oki, Dominique Schols

Open access · greenAbstract 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 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

40 citing papers in PubMed, 103 citations in OpenAlex.

  1. Carbohydrate-Binding Mechanism and Therapeutic Potential of Lectin Mimics.Advances in experimental medicine and biology · 2026
    Review
  2. Genomic Insights intoJournal of microbiology and biotechnology · 2023
    Article
  3. Article
  4. Sensing the interactions between carbohydrate-binding agents andJournal of biomolecular structure & dynamics · 2022
    Article
  5. Lectins and lectibodies: potential promising antiviral agents.Cellular & molecular biology letters · 2022
    Review
  6. Mannose-binding analysis and biological application of pradimicins.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Complement Protein C1q Interacts with DC-SIGNFrontiers in immunology · 2016
    Article
  14. Article
  15. Article
  16. Article
  17. Synergistic actions of tailoring enzymes in pradimicin biosynthesis.Chembiochem : a European journal of chemical biology · 2014
    Article
  18. Review
  19. Article
  20. Review
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

9 authors at 5 institutions in 4 countries.

Jan BalzariniRega Institute for Medical Research, Minderbroedersstraat 10, B-3000 Leuven, Belgium. jan.balzarini@rega.kuleuven.ac.be
Kristel Van Laethem
Dirk Daelemans
Sigrid Hatse
Antonella Bugatti
Marco Rusnati
Yasuhiro Igarashi
Toshikazu Oki
Dominique Schols
Rega Institute for Medical Research · BEKU Leuven · BEUniversity of Brescia · ITToyama Prefectural University · JPUniversity of Southern California · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pradimicin A (PRM-A), an antifungal nonpeptidic benzonaphtacenequinone antibiotic, is a low-molecular-weight (molecular weight, 838) carbohydrate binding agent (CBA) endowed with a selective inhibitory activity against human immunodeficiency virus (HIV). It invariably inhibits representative virus strains of a variety of HIV-1 clades with X4 and R5 tropisms at nontoxic concentrations. Time-of-addition studies revealed that PRM-A acts as a true virus entry inhibitor. PRM-A specifically interacts with HIV-1 gp120 and efficiently prevents virus transmission in cocultures of HUT-78/HIV-1 and Sup T1 cells. Upon prolonged exposure of HIV-1-infected CEM cell cultures, PRM-A drug pressure selects for mutant HIV-1 strains containing N-glycosylation site deletions in gp120 but not gp41. A relatively long exposure time to PRM-A is required before drug-resistant virus strains emerge. PRM-A has a high genetic barrier, since more than five N-glycosylation site deletions in gp120 are required to afford moderate drug resistance. Such mutated virus strains keep full sensitivity to the other known clinically used anti-HIV drugs. PRM-A represents the first prototype compound of a nonpeptidic CBA lead and, together with peptide-based lectins, belongs to a conceptually novel type of potential therapeutics for which drug pressure results in the selection of glycan deletions in the HIV gp120 envelope.

Indexed as

AnthracyclinesAnti-HIV AgentsCarbohydrate MetabolismCD4 AntigensCell LineCoculture TechniquesDrug Resistance, ViralGenotypeGlycosylationHIV-1HIV Envelope Protein gp120HumansModels, MolecularMutationPradimicins and BenanomicinsReceptors, CXCR4AnthracyclinesAnti-HIV AgentsCD4 AntigensHIV Envelope Protein gp120pradimicin APradimicins and BenanomicinsReceptors, CXCR4Viral Envelope Proteins

Identifiers

PMID17050611
PMCPMC1797273
OpenAlexW2118586318

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.