Evidence map›Paper›PMID 37054948›Full record

ArticleNew biotechnology2023

An approach to rapid distributed manufacturing of broad spectrum anti-viral griffithsin using cell-free systems to mitigate pandemics.

Shayan G Borhani, Max Z Levine, Lauren H Krumpe, Jennifer Wilson, Curtis J Henrich, Barry R O'Keefe, Donald C Lo, G Sitta Sittampalam, Alexander G Godfrey, R Dwayne Lunsford and 7 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in New biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

  1. Article
  2. Review
  3. Algal Lectin Griffithsin Inhibits Ebola Virus Infection.Molecules (Basel, Switzerland) · 2025
    Article
  4. Article
  5. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

17 authors.

Shayan G BorhaniCenter for Advanced Sensor Technology, Department of Chemical, Biochemical and Environmental Engineering, University of Maryland Baltimore County, Baltimore, MD 21250, USA; Department of Chemical, Biochemical and Environmental Engineering, University of Maryland Baltimore County, Baltimore, MD 21250, USA.
Max Z LevineDepartment of Chemical Engineering and Department of Bioengineering, Stanford University, Stanford, CA 94305-5025, USA.
Lauren H KrumpeMolecular Targets Program, Center for Cancer Research, NCI-Frederick, NIH, Frederick, MD 21702, USA; Basic Science Program, Leidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research, Frederick, MD 21702, USA.
Jennifer WilsonMolecular Targets Program, Center for Cancer Research, NCI-Frederick, NIH, Frederick, MD 21702, USA.
Curtis J HenrichMolecular Targets Program, Center for Cancer Research, NCI-Frederick, NIH, Frederick, MD 21702, USA; Basic Science Program, Leidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research, Frederick, MD 21702, USA.
Barry R O'KeefeMolecular Targets Program, Center for Cancer Research, NCI-Frederick, NIH, Frederick, MD 21702, USA; Natural Products Branch, Developmental Therapeutics Program, Division of Cancer Treatment and Diagnosis, National Cancer Institute, Frederick, MD 21702, USA.
Donald C LoNational Center for Advancing Translational Sciences, National Institutes of Health, 9800 Medical Center Drive, Rockville, MD 20850, USA.
G Sitta SittampalamNational Center for Advancing Translational Sciences, National Institutes of Health, 9800 Medical Center Drive, Rockville, MD 20850, USA.
Alexander G GodfreyBasic Science Program, Leidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research, Frederick, MD 21702, USA.
R Dwayne LunsfordNational Center for Advancing Translational Sciences, National Institutes of Health, 9800 Medical Center Drive, Rockville, MD 20850, USA.
Venkata MangalampalliNational Center for Advancing Translational Sciences, National Institutes of Health, 9800 Medical Center Drive, Rockville, MD 20850, USA.
Dingyin TaoNational Center for Advancing Translational Sciences, National Institutes of Health, 9800 Medical Center Drive, Rockville, MD 20850, USA.
Christopher A LeClairNational Center for Advancing Translational Sciences, National Institutes of Health, 9800 Medical Center Drive, Rockville, MD 20850, USA.
Aaron P TholeCenter for Advanced Sensor Technology, Department of Chemical, Biochemical and Environmental Engineering, University of Maryland Baltimore County, Baltimore, MD 21250, USA; Department of Chemical, Biochemical and Environmental Engineering, University of Maryland Baltimore County, Baltimore, MD 21250, USA.
Douglas FreyCenter for Advanced Sensor Technology, Department of Chemical, Biochemical and Environmental Engineering, University of Maryland Baltimore County, Baltimore, MD 21250, USA; Department of Chemical, Biochemical and Environmental Engineering, University of Maryland Baltimore County, Baltimore, MD 21250, USA.
James SwartzDepartment of Chemical Engineering and Department of Bioengineering, Stanford University, Stanford, CA 94305-5025, USA.
Govind RaoCenter for Advanced Sensor Technology, Department of Chemical, Biochemical and Environmental Engineering, University of Maryland Baltimore County, Baltimore, MD 21250, USA; Department of Chemical, Biochemical and Environmental Engineering, University of Maryland Baltimore County, Baltimore, MD 21250, USA. Electronic address: grao@umbc.edu.

Funding

Research Services Section (RSS)ZICTR000242 · NCATS · NATIONAL CENTER FOR ADVANCING TRANSLATIONAL SCIENCES · PI WILSON, KELLI · 2015 to 2025
$64.9M
Analytical ChemistryZICTR000037 · NCATS · NATIONAL CENTER FOR ADVANCING TRANSLATIONAL SCIENCES · PI LECLAIR, CHRISTOPHER ARTHUR · 2015 to 2025
$23.2M
Isolation of bioactive proteins from natural product extractsZIABC011472 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI OKEEFE, BARRY · 2012 to 2025
$7.8M
CCR NIH HHS HHSN261200800001CNCI NIH HHS HHSN261200800001E
6 · The paper itself

Abstract

This study describes the cell-free biomanufacturing of a broad-spectrum antiviral protein, griffithsin (GRFT) such that it can be produced in microgram quantities with consistent purity and potency in less than 24 h. We demonstrate GRFT production using two independent cell-free systems, one plant and one microbial. Griffithsin purity and quality were verified using standard regulatory metrics. Efficacy was demonstrated in vitro against SARS-CoV-2 and HIV-1 and was nearly identical to that of GRFT expressed in vivo. The proposed production process is efficient and can be readily scaled up and deployed wherever a viral pathogen might emerge. The current emergence of viral variants of SARS-CoV-2 has resulted in frequent updating of existing vaccines and loss of efficacy for front-line monoclonal antibody therapies. Proteins such as GRFT with its efficacious and broad virus neutralizing capability provide a compelling pandemic mitigation strategy to promptly suppress viral emergence at the source of an outbreak.

Indexed as

Antiviral AgentsCOVID-19Cell-Free SystemHumansPandemicsPlant LectinsSARS-CoV-2Antiviral Agentsgriffithsin protein, GriffithsiaPlant LectinsAntiviral griffithsinCell-free protein synthesis (CFPS)Distributed manufacturingPandemic preparednessSARS-CoV-2

Identifiers

PMID37054948
PMCPMC10330340

What OpenQuestion holds

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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.