Evidence map›Paper›PMID 20160016›Full record

ArticleInfection and immunity2010

Leptospiral endostatin-like protein A is a bacterial cell surface receptor for human plasminogen.

Ashutosh Verma, Catherine A Brissette, Amy A Bowman, Samir T Shah, Peter F Zipfel, Brian Stevenson

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
7.6field-weighted citation impact, top 2% 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

44 citing papers in PubMed, 93 citations in OpenAlex.

  1. Review
  2. The Leptospira interrogans proteome's response to zinc highlights the potential involvement of this metal in translational-machinery and virulence.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024
    Article
  3. Unveiling the impact ofInfection and immunity · 2024
    Article
  4. Article
  5. Subversion of the immune response of human pathogenic spirochetes.Journal of clinical laboratory analysis · 2022
    Review
  6. Review
  7. Article
  8. Article
  9. AAA+ Molecular Chaperone ClpB inInternational journal of molecular sciences · 2020
    Review
  10. Article
  11. Review
  12. Frontiers in cellular and infection microbiology · 2018
    Article
  13. Article
  14. Article
  15. Complement Evasion by PathogenicFrontiers in immunology · 2016
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. The leptospiral outer membrane.Current topics in microbiology and immunology · 2015
    Review
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

6 authors at 2 institutions in 2 countries.

Ashutosh VermaDepartment of Microbiology, Immunology, and Molecular Genetics, University of Kentucky College of Medicine, MN 469 Chandler Medical Center, Lexington, KY 40536-0298, USA. ashutosh.verma@uky.edu
Catherine A Brissette
Amy A Bowman
Samir T Shah
Peter F Zipfel
Brian Stevenson
University of Kentucky · USLeibniz-Institut für Naturstoff-Forschung und Infektionsbiologie e. V. - Hans-Knöll-Institut (HKI) · DE

Funding

Leptospira interrogans Len adhesinsR21AI078111 · NIAID · UNIVERSITY OF KENTUCKY · PI STEVENSON, BRIAN · 2008 to 2009
$403k
NIAID NIH HHS AI-78111NIAID NIH HHS R21 AI078111
6 · The paper itself

Abstract

The spirochete Leptospira interrogans is a highly invasive pathogen of worldwide public health importance. Studies from our laboratories and another have demonstrated that L. interrogans can acquire host plasminogen on its surface. Exogenous plasminogen activators can then convert bound plasminogen into the functionally active protease plasmin. In this study, we extend upon those observations and report that leptospiral endostatin-like protein A (LenA) binds human plasminogen in a dose-dependent manner. LenA-plasminogen interactions were significantly inhibited by the lysine analog xi-aminocaproic acid, suggesting that the lysine-binding sites on the amino-terminal kringle portion of the plasminogen molecule play a role in the binding. Previous studies have shown that LenA also binds complement regulator factor H and the extracellular matrix component laminin. Plasminogen competed with both factor H and laminin for binding to LenA, which suggests overlapping ligand-binding sites on the bacterial receptor. Finally, LenA-bound plasminogen could be converted to plasmin, which in turn degraded fibrinogen, suggesting that acquisition of host-derived plasmin by LenA may aid bacterial dissemination throughout host tissues.

Indexed as

AminocaproatesBacterial ProteinsComplement Factor HEnzyme InhibitorsHumansLamininLeptospira interrogansPlasminogenProtein BindingProtein Interaction MappingAminocaproatesBacterial ProteinsComplement Factor HEnzyme InhibitorsLamininPlasminogen

Identifiers

PMID20160016
PMCPMC2863546
OpenAlexW2115743884

What OpenQuestion holds

Textmetadata
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.