Evidence map›Paper›PMID 20961853›Full record

ArticleThe Journal of biological chemistry2011

The oligopeptidase B of Leishmania regulates parasite enolase and immune evasion.

Ryan K Swenerton, Shuyi Zhang, Mohammed Sajid, Katalin F Medzihradszky, Charles S Craik, Ben L Kelly, James H McKerrow

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
8.5field-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

42 citing papers in PubMed, 91 citations in OpenAlex.

  1. LABCG1 AffectsACS infectious diseases · 2026
    Article
  2. Surface enolase is a virulence factor ofFrontiers in microbiology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Characterization ofParasitology · 2022
    Article
  12. Article
  13. Novel Insights IntoFrontiers in cellular and infection microbiology · 2022
    Article
  14. Article
  15. Article
  16. Insights intoVeterinary sciences · 2021
    Review
  17. Prolyl Oligopeptidase FromFrontiers in microbiology · 2020
    Article
  18. Flavopereirine-An Alkaloid Derived fromMolecules (Basel, Switzerland) · 2019
    Article
  19. Review
  20. 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

7 authors at 3 institutions in 2 countries.

Ryan K SwenertonDepartment of Pathology, Sandler Center for Drug Discovery, University of California, San Francisco, California 94158, USA.
Shuyi Zhang
Mohammed Sajid
Katalin F Medzihradszky
Charles S Craik
Ben L Kelly
James H McKerrow
University of California, San Francisco · USLeiden University · NLLouisiana State University Health Sciences Center New Orleans · US

Funding

YEAST THREONINE &SERINE KINASESP41RR001614 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SZOKA, FRANCIS C. · 1985 to 2011
$24.1M
X-RAY CRYSTALLOGRAPHYP01AI035707 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MCKERROW, JAMES H. · 1995 to 2008
$7.8M
PURCHASE OF Q TOF MASS SPECTROMETERS10RR012961 · NCRR · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI JAMES, THOMAS L · 1998 to 1998
–
NCRR NIH HHS P41 RR001614NCRR NIH HHS P41RR001614NCRR NIH HHS RR012961NIAID NIH HHS AI35707NIAID NIH HHS P01 AI035707
6 · The paper itself

Abstract

Proteases are a ubiquitous group of enzymes that play key roles in the life cycle of parasites, in the host-parasite relationship, and in the pathogenesis of parasitic diseases. Furthermore, proteases are targets for the development of new anti-parasitic therapy. Protozoan parasites like Leishmania predominantly express Clan CA cysteine proteases for key life cycle functions. It was therefore unexpected to find a high level of serine protease activity expressed by Leishmania donovani. Purification of this activity followed by mass spectrometry identified oligopeptidase B (OPB; Clan SC, family S9A) as the responsible enzyme. This was confirmed by gene knock-out of OPB, which resulted in the disappearance of the detected serine protease activity of Leishmania extracts. To delineate the specific role of OPB in parasite physiology, proteomic analysis was carried out on OPB(-/-) versus wild type parasites. Four protein species were significantly elevated in OPB(-/-) parasites, and all four were identified by mass spectrometry as enolase. This increased enolase was enzymatically inactive and associated with the parasite membrane. Aside from its classic role in carbohydrate metabolism, enolase was recently found to localize to membranes, where it binds host plasminogen and functions as a virulence factor for several pathogens. As expected, there was a striking alteration in macrophage responses to Leishmania when OPB was deleted. Whereas wild type parasites elicited little, if any, response from infected macrophages, OPB(-/-) parasites induced a massive up-regulation in gene transcription. Additionally, these OPB(-/-) parasites displayed decreased virulence in the murine footpad infection model.

Indexed as

Immune EvasionAnimalsCloning, MolecularFemaleGene DeletionLeishmania donovaniLeishmaniasis, VisceralLife Cycle StagesMacrophagesMiceMice, Inbred BALB CMolecular Sequence DataPeptide HydrolasesPhosphopyruvate HydratasePichiaProtein IsoformsPeptide HydrolasesPhosphopyruvate HydrataseProtein IsoformsProteomeRecombinant ProteinsSerine Proteases

Identifiers

PMID20961853
PMCPMC3013002
OpenAlexW2112315287

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.