Evidence map›Paper›PMID 21283773›Full record

ArticlePloS one2011

HIV-1 enhancing effect of prostatic acid phosphatase peptides is reduced in human seminal plasma.

Julie A Martellini, Amy L Cole, Pavel Svoboda, Olga Stuchlik, Li-Mei Chen, Karl X Chai, Bhushan K Gangrade, Ole E Sørensen, Jan Pohl, Alexander M Cole

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

19 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Semen-derived amyloidogenic peptides-Key players of HIV infection.Protein science : a publication of the Protein Society · 2018
    Review
  6. Human Semen or Seminal Plasma Does Not Enhance HIV-1AIDS research and human retroviruses · 2018
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Mycoplasma genitalium promotes epithelial crossing and peripheral blood mononuclear cell infection by HIV-1.International journal of infectious diseases : IJID : official publication of the International Society for Infectious Diseases · 2014
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
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

10 authors at 3 institutions in 2 countries.

Julie A MartelliniDepartment of Molecular Biology & Microbiology, Biomolecular Science Center, Burnett School of Biomedical Sciences at the University of Central Florida College of Medicine, Orlando, Florida, United States of America.
Amy L Cole
Pavel Svoboda
Olga Stuchlik
Li-Mei Chen
Karl X Chai
Bhushan K Gangrade
Ole E Sørensen
Jan Pohl
Alexander M Cole
University of Central Florida · USCenters for Disease Control and Prevention · USLund University · SE

Funding

ORGAN CULTURE TO TEST MICROBICIDESU19AI065430 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI CUMMINS, JAMES E. · 2005 to 2008
$4.9M
Retrocyclins: Circular Defensins Active Against HIV-1R01AI052017 · NIAID · UNIVERSITY OF CENTRAL FLORIDA · PI COLE, ALEXANDER MICHAEL · 2002 to 2010
$3.0M
NIAID NIH HHS R01 AI052017NIAID NIH HHS U19 AI065430
6 · The paper itself

Abstract

We recently reported that HIV-1 infection can be inhibited by innate antimicrobial components of human seminal plasma (SP). Conversely, naturally occurring peptidic fragments from the SP-derived prostatic acid phosphatase (PAP) have been reported to form amyloid fibrils called "SEVI" and enhance HIV-1 infection in vitro. In order to understand the biological consequence of this proviral effect, we extended these studies in the presence of human SP. PAP-derived peptides were agitated to form SEVI and incubated in the presence or absence of SP. While PAP-derived peptides and SEVI alone were proviral, the presence of 1% SP ablated their proviral activity in several different anti-HIV-1 assays. The anti-HIV-1 activity of SP was concentration dependent and was reduced following filtration. Supraphysiological concentrations of PAP peptides and SEVI incubated with diluted SP were degraded within hours, with SP exhibiting proteolytic activity at dilutions as high as 1:200. Sub-physiological concentrations of two prominent proteases of SP, prostate-specific antigen (PSA) and matriptase, could degrade physiological and supraphysiological concentrations of PAP peptides and SEVI. While human SP is a complex biological fluid, containing both antiviral and proviral factors, our results suggest that PAP peptides and SEVI may be subject to naturally occurring proteolytic components capable of reducing their proviral activity.

Indexed as

Acid PhosphataseAmyloidDose-Response Relationship, DrugHIV-1HIV EnhancerHumansPeptide FragmentsProstate-Specific AntigenProtein Tyrosine PhosphatasesSemenSerine EndopeptidasesAcid PhosphataseAmyloidmatriptasePeptide FragmentsProstate-Specific Antigenprostatic acid phosphataseProtein Tyrosine PhosphatasesSerine Endopeptidases

Identifiers

PMID21283773
PMCPMC3024420
OpenAlexW2000037909

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.