Evidence map›Paper›PMID 22239120›Full record

ArticleJournal of the American Chemical Society2012

Oligovalent amyloid-binding agents reduce SEVI-mediated enhancement of HIV-1 infection.

Christina C Capule, Caitlin Brown, Joanna S Olsen, Stephen Dewhurst, Jerry Yang

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.2field-weighted citation impact, top 25% 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

23 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
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  6. Review
  7. Article
  8. Structure, function and antagonism of semen amyloids.Chemical communications (Cambridge, England) · 2018
    Review
  9. Semen-derived amyloidogenic peptides-Key players of HIV infection.Protein science : a publication of the Protein Society · 2018
    Review
  10. Article
  11. Article
  12. Review
  13. Article
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  15. 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

5 authors at 2 institutions in 1 country.

Christina C CapuleDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093-0358, USA.
Caitlin Brown
Joanna S Olsen
Stephen Dewhurst
Jerry Yang
University of Rochester · USUniversity of California, San Diego · US

Funding

University of Rochester Mentoring Environment: Nurturing Training Opportunities in Research (UR-MENTOR)T32GM007356 · NIGMS · UNIVERSITY OF ROCHESTER · PI O'BANION, M. KERRY · 1985 to 2023
$15.1M
Virology/Immunology CoreP30AI078498 · NIAID · UNIVERSITY OF ROCHESTER · PI DEWHURST, STEPHEN · 2008 to 2018
$14.6M
PHARMACOLOGY OF DRUG ABUSET32DA007232 · NIDA · UNIVERSITY OF ROCHESTER · PI BIDLACK, JEAN M · 1985 to 2011
$2.1M
The Semen Enhancer of HIV Infection as a Novel Microbicide TargetR21AI094511 · NIAID · UNIVERSITY OF ROCHESTER · PI DEWHURST, STEPHEN · 2011 to 2012
$434k
Acquisition of a High Resolution TOF Mass SpectrometerS10RR025636 · NCRR · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI MOLINSKI, TADEUSZ F · 2010 to 2010
$305k
NCRR NIH HHS 1S10RR025636-01A1NCRR NIH HHS S10 RR025636NIAID NIH HHS P30 AI078498NIAID NIH HHS P30AI078498NIAID NIH HHS R21 AI094511NIAID NIH HHS R21AI094511NIDA NIH HHS T32 DA007232NIDA NIH HHS T32DA007232NIGMS NIH HHS T32 GM007356NIGMS NIH HHS T32GM007356
6 · The paper itself

Abstract

This paper evaluates the use of oligovalent amyloid-binding molecules as potential agents that can reduce the enhancement of human immunodeficiency virus-1 (HIV-1) infection in cells by semen-derived enhancer of virus infection (SEVI) fibrils. These naturally occurring amyloid fibrils found in semen have been implicated as mediators that can facilitate the attachment and internalization of HIV-1 virions to immune cells. Molecules that are capable of reducing the role of SEVI in HIV-1 infection may, therefore, represent a novel strategy to reduce the rate of sexual transmission of HIV-1 in humans. Here, we evaluated a set of synthetic, oligovalent derivatives of benzothiazole aniline (BTA, a known amyloid-binding molecule) for their capability to bind cooperatively to aggregated amyloid peptides and to neutralize the effects of SEVI in HIV-1 infection. We demonstrate that these BTA derivatives exhibit a general trend of increased binding to aggregated amyloids as a function of increasing valence number of the oligomer. Importantly, we find that oligomers of BTA show improved capability to reduce SEVI-mediated infection of HIV-1 in cells compared to a BTA monomer, with the pentamer exhibiting a 65-fold improvement in efficacy compared to a previously reported monomeric BTA derivative. These results, thus, support the use of amyloid-targeting molecules as potential supplements for microbicides to curb the spread of HIV-1 through sexual contact.

Indexed as

AmyloidAniline CompoundsAnti-Infective AgentsBenzothiazolesCD4 AntigensCell LineHIV-1HumansReceptors, CCR5Receptors, CXCR4SemenVirus AttachmentAmyloidAniline CompoundsAnti-Infective AgentsBenzothiazolesCD4 AntigensCXCR4 protein, humanReceptors, CCR5Receptors, CXCR4

Identifiers

PMID22239120
PMCPMC3262105
OpenAlexW1973046776

What OpenQuestion holds

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LicenceTDM
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.