Evidence map›Paper›PMID 20559567›Full record

ArticlePloS one2010

HIV-1 neutralization profile and plant-based recombinant expression of actinohivin, an Env glycan-specific lectin devoid of T-cell mitogenic activity.

Nobuyuki Matoba, Adam S Husk, Brian W Barnett, Michelle M Pickel, Charles J Arntzen, David C Montefiori, Atsushi Takahashi, Kazunobu Tanno, Satoshi Omura, Huyen Cao and 3 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
4.7field-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

21 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
  2. Review
  3. Lectins and lectibodies: potential promising antiviral agents.Cellular & molecular biology letters · 2022
    Review
  4. Antitumor activity of a lectibody targeting cancer-associated high-mannose glycans.Molecular therapy : the journal of the American Society of Gene Therapy · 2022
    Article
  5. Engineering of a Lectibody Targeting High-Mannose-Type Glycans of the HIV Envelope.Molecular therapy : the journal of the American Society of Gene Therapy · 2019
    Article
  6. Review
  7. Article
  8. [Transient expression of bioactive recombinant human plasminogen activator in tobacco leaf].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2019
    Article
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  11. Review
  12. Review
  13. Review
  14. Article
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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

13 authors at 7 institutions in 2 countries.

Nobuyuki MatobaOwensboro Cancer Research Program, Owensboro, Kentucky, United States of America. n.matoba@louisville.edu
Adam S Husk
Brian W Barnett
Michelle M Pickel
Charles J Arntzen
David C Montefiori
Atsushi Takahashi
Kazunobu Tanno
Satoshi Omura
Huyen Cao
Jason P Mooney
Carl V Hanson
Haruo Tanaka
California Department of Public Health · USArizona State University · USIwaki Meisei University · JPOwensboro Health · USDuke Medical Center · USKitasato University · JPUniversity of Louisville · US

Funding

NIAID NIH HHS N01 AI030034
6 · The paper itself

Abstract

The development of a topical microbicide blocking the sexual transmission of HIV-1 is urgently needed to control the global HIV/AIDS pandemic. The actinomycete-derived lectin actinohivin (AH) is highly specific to a cluster of high-mannose-type glycans uniquely found on the viral envelope (Env). Here, we evaluated AH's candidacy toward a microbicide in terms of in vitro anti-HIV-1 activity, potential side effects, and recombinant producibility. Two validated assay systems based on human peripheral blood mononuclear cell (hPBMC) infection with primary isolates and TZM-bl cell infection with Env-pseudotyped viruses were employed to characterize AH's anti-HIV-1 activity. In hPMBCs, AH exhibited nanomolar neutralizing activity against primary viruses with diverse cellular tropisms, but did not cause mitogenicity or cytotoxicity that are often associated with other anti-HIV lectins. In the TZM-bl-based assay, AH showed broad anti-HIV-1 activity against clinically-relevant, mucosally transmitting strains of clades B and C. By contrast, clade A viruses showed strong resistance to AH. Correlation analysis suggested that HIV-1's AH susceptibility is significantly linked to the N-glycans at the Env C2 and V4 regions. For recombinant (r)AH expression, we evaluated a tobacco mosaic virus-based system in Nicotiana benthamiana plants as a means to facilitate molecular engineering and cost-effective mass production. Biochemical analysis and an Env-mediated syncytium formation assay demonstrated high-level expression of functional rAH within six days. Taken together, our study revealed AH's cross-clade anti-HIV-1 activity, apparent lack of side effects common to lectins, and robust producibility using plant biotechnology. These findings justify further efforts to develop rAH toward a candidate HIV-1 microbicide.

Indexed as

Neutralization TestsBacterial ProteinsCell ProliferationHeLa CellsHIV-1HumansMitogensNicotianaRecombinant ProteinsT-Lymphocytesactinohivin protein, actinomyceteBacterial ProteinsMitogensRecombinant Proteins

Identifiers

PMID20559567
PMCPMC2886112
OpenAlexW2065533760

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.