Evidence map›Paper›PMID 24600566›Full record

ArticleResults in immunology2013

Complement regulator C4BP binds to Staphylococcus aureus surface proteins SdrE and Bbp inhibiting bacterial opsonization and killing.

Pamela S Hair, Caitlin K Foley, Neel K Krishna, Julius O Nyalwidhe, Joan A Geoghegan, Timothy J Foster, Kenji M Cunnion

Open access · hybridAbstract read
In one paragraph

Article in Results in immunology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Article
  3. Diverse Functions of C4b-Binding Protein in Health and Disease.Journal of immunology (Baltimore, Md. : 1950) · 2023
    Review
  4. Article
  5. Article
  6. Article
  7. Innate immune evasion of Escherichia coli clinical strains from orthopedic implant infections.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2016
    Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Complement System Part II: Role in Immunity.Frontiers in immunology · 2015
    Review
  14. 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.

Pamela S HairDepartment of Pediatrics, Eastern Virginia Medical School, 855 West Brambleton Avenue, P.O. Box 1980, Norfolk, VA 23501-1980, USA.
Caitlin K FoleyDepartment of Pediatrics, Eastern Virginia Medical School, 855 West Brambleton Avenue, P.O. Box 1980, Norfolk, VA 23501-1980, USA.
Neel K KrishnaDepartment of Microbiology and Molecular Cell Biology, Eastern Virginia Medical School, 700 West Olney Road, Norfolk, VA, USA.
Julius O NyalwidheDepartment of Microbiology and Molecular Cell Biology, Eastern Virginia Medical School, 700 West Olney Road, Norfolk, VA, USA ; Leroy T. Canoles Jr. Cancer Research Center, Eastern Virginia Medical School, 651 Colley Avenue, Norfolk, VA, USA.
Joan A GeogheganDepartment of Microbiology, Trinity College, The University of Dublin, Dublin, Ireland.
Timothy J FosterDepartment of Microbiology, Trinity College, The University of Dublin, Dublin, Ireland.
Kenji M CunnionDepartment of Pediatrics, Eastern Virginia Medical School, 855 West Brambleton Avenue, P.O. Box 1980, Norfolk, VA 23501-1980, USA ; Children's Specialty Group, 601 Children's Lane, Norfolk, VA, USA ; The Children's Hospital of The King's Daughters, 601 Children's Lane, Norfolk, VA, USA.
Eastern Virginia Medical School · USTrinity College Dublin · IEChildren's Hospital of The King's Daughters · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Staphylococcus aureus is a premier human pathogen and the most common cause of osteoarticular, wound, and implanted device infections. We recently demonstrated S. aureus efficiently binds the classical complement regulator C4b-binding protein (C4BP) inhibiting antibody-initiated complement-mediated opsonization. Here we identify S. aureus surface protein SdrE as a C4BP-binding protein. Recombinant SdrE and recombinant bone sialoprotein-binding protein (Bbp), an allelic variant of SdrE, both efficiently bound to C4BP in heat-inactivated human serum. We previously described SdrE as binding alternative pathway regulator factor H. Recombinant SdrE and Bbp efficiently bound C4BP and factor H in serum without apparent interference. Gain of function studies utilizing Lactococcus lactis clones expressing SdrE or Bbp increased serum C4BP and factor H binding, compared with empty-vector control (WT) approximately 2-fold. Correspondingly, classical pathway-mediated C3-fragment opsonization and bacterial killing by human neutrophils decreased by half for L. lactis clones expressing SdrE or Bbp compared with WT. In summary, we identify SdrE and allelic variant Bbp as S. aureus surface proteins that bind the complement regulator C4BP inhibiting classical pathway-mediated bacterial opsonization and killing.

Indexed as

C4BPComplementOpsonophagocytosisSdrEStaphylococcus aureus

Identifiers

PMID24600566
PMCPMC3908334
OpenAlexW2037144971

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.