Evidence map›Paper›PMID 14638802›Full record

ArticleInfection and immunity2003

Recruitment of complement factor H-like protein 1 promotes intracellular invasion by group A streptococci.

Vinod Pandiripally, Lin Wei, Christine Skerka, Peter F Zipfel, David Cue

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
6.8field-weighted citation impact, top 3% 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

26 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Intracellular Invasion byMicrobiology spectrum · 2019
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Acquisition of factor H by a novel surface protein on group B Streptococcus promotes complement degradation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2009
    Article
  14. Article
  15. Article
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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

5 authors at 2 institutions in 2 countries.

Vinod PandiripallyDepartment of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City 66160, USA.
Lin Wei
Christine Skerka
Peter F Zipfel
David Cue
University of Kansas Medical Center · USLeibniz-Institut für Naturstoff-Forschung und Infektionsbiologie e. V. - Hans-Knöll-Institut (HKI) · DE

Funding

XRAY CRYSTALLOGRAPHY CORE (JANUARY 1 - JUNE 30, 2005)P20RR016443 · NCRR · UNIVERSITY OF KANSAS MEDICAL CENTER · PI VINES, CHARLOTTE M · 2001 to 2010
$21.3M
NCRR NIH HHS P20 RR016443NCRR NIH HHS P20RR16443-03
6 · The paper itself

Abstract

Numerous microbial pathogens exploit complement regulatory proteins such as factor H (FH) and factor H-like protein 1 (FHL-1) for immune evasion. Fba is an FHL-1 and FH binding protein expressed on the surface of the human pathogenic bacterium, Streptococcus pyogenes, a common agent of pharyngeal, skin, and soft-tissue infections. In the present study, we demonstrate that Fba and FHL-1 work in concert to promote invasion of epithelial cells by S. pyogenes. Fba fragments were expressed as recombinant proteins and assayed for binding of FHL-1 and FH by Western blotting, enzyme-linked immunosorbent assay, and surface plasmon resonance. A binding site for FHL-1 and FH was localized to the N-terminal half of Fba, a region predicted to contain a coiled-coil domain. Deletion of this coiled-coil domain greatly reduced FHL-1 and FH binding. PepSpot analyses identified a 16-amino-acid segment of Fba which overlaps the coiled-coil domain that binds both FHL-1 and FH. To localize the Fba binding site in FHL-1 and FH, surface plasmon resonance was used to assess the interactions between the streptococcal protein and a series of recombinant FH deletion constructs. The Fba binding site was localized to short consensus repeat 7 (SCR 7), a domain common to FHL-1 and FH. SCR 7 contains a heparin binding site, and heparin was found to inhibit FHL-1 binding to Fba. FHL-1 promoted entry of Fba(+) group A streptococci into epithelial cells in a dose-dependent manner but did not affect invasion by an isogenic fba mutant. To our knowledge, this is the first report of a bacterial pathogen exploiting a soluble complement regulatory protein for entry into host cells.

Indexed as

Bacterial ProteinsBinding SitesBlood ProteinsCarrier ProteinsCell LineComplement ActivationComplement Factor HEpithelial CellsFructose-Bisphosphate AldolaseHumansLungRecombinant ProteinsStreptococcus pyogenesBacterial ProteinsBlood ProteinsCarrier ProteinsCFH protein, humanComplement Factor Hfactor H-related protein 1Fba protein, Streptococcus pyogenesFructose-Bisphosphate AldolaseRecombinant Proteins

Identifiers

PMID14638802
PMCPMC308943
OpenAlexW1977663109

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.