Evidence map›Paper›PMID 27783038›Full record

ReviewViruses2016

Griffithsin: An Antiviral Lectin with Outstanding Therapeutic Potential.

Sabrina Lusvarghi, Carole A Bewley

Open access · goldAbstract readReview
In one paragraph

Review in Viruses, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

90 citing papers in PubMed, 152 citations in OpenAlex.

  1. Review
  2. Article
  3. Innate Immunity and Microbial Recognition in Reproduction: From Barrier Defense to Maternal-Fetal Tolerance.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Review
  4. Review
  5. Review
  6. In Vitro Antiviral Activity of Red Algae Extracts fromTropical medicine and infectious disease · 2026
    Article
  7. Article
  8. Article
  9. Review
  10. An engineered antibody-lectin conjugate targeting the HIV glycan shield protects humanized mice against HIV challenge.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
    Article
  11. Nipah virus: pathogenesis, genome, diagnosis, and treatment.Applied microbiology and biotechnology · 2025
    Review
  12. Article
  13. Algal Lectin Griffithsin Inhibits Ebola Virus Infection.Molecules (Basel, Switzerland) · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Antiviral Protein-Protein Interaction Inhibitors.Journal of medicinal chemistry · 2024
    Review
  20. Review

30 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Sabrina LusvarghiLaboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA. sabrinal@mail.nih.gov.
Carole A BewleyLaboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA. caroleb@mail.nih.gov.
National Institute of Diabetes and Digestive and Kidney Diseases · USNational Institutes of Health · US

Funding

Inhibitors and Probes of HIV-1 Cell FusionZIADK032103 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BEWLEY, CAROLE · 2009 to 2025
$12.5M
6 · The paper itself

Abstract

Griffithsin (GRFT), an algae-derived lectin, is one of the most potent viral entry inhibitors discovered to date. It is currently being developed as a microbicide with broad-spectrum activity against several enveloped viruses. GRFT can inhibit human immunodeficiency virus (HIV) infection at picomolar concentrations, surpassing the ability of most anti-HIV agents. The potential to inhibit other viruses as well as parasites has also been demonstrated. Griffithsin's antiviral activity stems from its ability to bind terminal mannoses present in high-mannose oligosaccharides and crosslink these glycans on the surface of the viral envelope glycoproteins. Here, we review structural and biochemical studies that established mode of action and facilitated construction of GRFT analogs, mechanisms that may lead to resistance, and in vitro and pre-clinical results that support the therapeutic potential of this lectin.

Indexed as

AnimalsAntiparasitic AgentsAntiviral AgentsDrug Evaluation, PreclinicalHumansMicrobial Sensitivity TestsPlant LectinsVirus InternalizationAntiparasitic AgentsAntiviral Agentsgriffithsin protein, GriffithsiaPlant Lectinscarbohydrate binding agentHCVHIVHSVimmunogenicitymultivalencyresistanceviral envelope glycoproteins

Identifiers

PMID27783038
PMCPMC5086628
OpenAlexW2532457307

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.