Evidence map›Paper›PMID 19114481›Full record

ArticleJournal of bacteriology2009

Streptococcus agalactiae CspA is a serine protease that inactivates chemokines.

Joshua D Bryan, Daniel W Shelver

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

27 citing papers in PubMed, 50 citations in OpenAlex.

  1. SpyCEP dismantles neutrophil immunity via disorder-driven chemokine remodeling and GAG targeting.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Virulence Factor Genes and Cytotoxicity ofMicrobiology spectrum · 2022
    Article
  7. Review
  8. Article
  9. Review
  10. Extracellular Pneumococcal Serine Proteases Affect Nasopharyngeal Colonization.Frontiers in cellular and infection microbiology · 2020
    Article
  11. Article
  12. Frontiers in immunology · 2018
    Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  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

2 authors at 1 institution in 1 country.

Joshua D BryanDepartment of Microbiology and Immunology, LSU Health Sciences Center in Shreveport, Shreveport, Louisiana 71130, USA.
Daniel W Shelver
Louisiana State University Health Sciences Center Shreveport · US

Funding

MtaR-regulated virulence in Streptococcus agalactiaeR21AI073818 · NIAID · LOUISIANA STATE UNIV HSC SHREVEPORT · PI SHELVER, DANIEL W · 2008 to 2009
$467k
Analysis of Group B Streptococcal Fibrinogen CleavageK22AI056271 · NIAID · LOUISIANA STATE UNIV HSC SHREVEPORT · PI SHELVER, DANIEL W · 2004 to 2005
$266k
NIAID NIH HHS K22 AI056271NIAID NIH HHS K22AI56271NIAID NIH HHS R21 AI073818NIAID NIH HHS R21AI073818
6 · The paper itself

Abstract

Streptococcus agalactiae (group B Streptococcus [GBS]) remains a leading cause of invasive infections in neonates and has emerged as a pathogen of the immunocompromised and elderly populations. The virulence mechanisms of GBS are relatively understudied and are still poorly understood. Previous evidence indicated that the GBS cspA gene is necessary for full virulence and the cleavage of fibrinogen. The predicted cspA product displays homology to members of the extracellular cell envelope protease family. CXC chemokines, many of which can recruit neutrophils to sites of infection, are important signaling peptides of the immune system. In this study, we purified CspA and demonstrated that it readily cleaved the CXC chemokines GRO-alpha, GRO-beta, GRO-gamma, neutrophil-activating peptide 2 (NAP-2), and granulocyte chemotactic protein 2 (GCP-2) but did not cleave interleukin-8. CspA did not cleave a panel of other test substrates, suggesting that it possesses a certain degree of specificity. CXC chemokines also underwent cleavage by whole GBS cells in a cspA-dependent manner. CspA abolished the abilities of three representative CXC chemokines, GRO-gamma, NAP-2, and GCP-2, to attract and activate neutrophils. Genetic and biochemical evidence indicated that CspA is a serine protease with S575 at its active site. D180 was also implicated as part of the signature serine protease catalytic triad, and both S575 and D180 were required for both N-terminal and C-terminal autocatalytic processing of CspA.

Indexed as

Bacterial ProteinsCatalytic DomainCells, CulturedChemokinesChemotaxisHumansNeutrophil ActivationNeutrophilsSerine EndopeptidasesStreptococcal InfectionsStreptococcus agalactiaeBacterial ProteinsChemokinesSerine Endopeptidases

Identifiers

PMID19114481
PMCPMC2648358
OpenAlexW2162470691

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.