Evidence map›Paper›PMID 7737120›Full record

ArticleThe EMBO journal1995

Protein H--a bacterial surface protein with affinity for both immunoglobulin and fibronectin type III domains.

I M Frick, K L Crossin, G M Edelman, L Björck

Open access · greenAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
4.5field-weighted citation impact, top 6% 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

25 citing papers in PubMed, 65 citations in OpenAlex.

  1. Interplay between group AMicrobiology and molecular biology reviews : MMBR · 2024
    Review
  2. Article
  3. A virological view of tenascin-C in infection.American journal of physiology. Cell physiology · 2023
    Review
  4. Review
  5. Article
  6. Group AMicrobiology spectrum · 2019
    Article
  7. Article
  8. Human IgG Increases Virulence ofJournal of immunology (Baltimore, Md. : 1950) · 2018
    Article
  9. Article
  10. Article
  11. SCM, the M Protein ofFrontiers in cellular and infection microbiology · 2017
    Article
  12. Article
  13. Review
  14. Review
  15. Streptococcus adherence and colonization.Microbiology and molecular biology reviews : MMBR · 2009
    Review
  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

4 authors at 1 institution in 1 country.

I M FrickDepartment of Medical and Physiological Chemistry, Lund University, Sweden.
K L Crossin
G M Edelman
L Björck
Lund University · SE

Funding

CELL-CELL ADHESION AMONG EMBRYONIC CELLSR01HD009635 · NICHD · SCRIPPS RESEARCH INSTITUTE, THE · PI EDELMAN, GERALD · 1985 to 2006
$2.6M
CELL-CELL ADHESION AMONG EMBRYONIC CELLSR37HD009635 · NICHD · SCRIPPS RESEARCH INSTITUTE · PI EDELMAN, GERALD · 1986 to 1996
–
NICHD NIH HHS HD-09635
6 · The paper itself

Abstract

Several bacterial species express surface proteins with affinity for the constant region (Fc) of immunoglobulin (Ig) G. The biological consequences of the interaction with IgG are poorly understood but it has been demonstrated that genes encoding different IgG Fc-binding proteins have undergone convergent evolution, suggesting that these surface molecules are connected with essential microbial functions. One of the molecules, protein H, is present in some strains of Streptococcus pyogenes, the most significant streptococcal species in clinical medicine. In contrast to other Ig-binding bacterial proteins tested, protein H was found to interact also with the neural cell adhesion molecule (N-CAM), a eukaryotic cell surface glycoprotein mediating homo- and heterophilic cell-cell interactions. The affinity for the interaction between protein H and N-CAM was 1.6 x 10(8)/M and the binding site on protein H was mapped to the NH2-terminal 80 amino acid residues. N-CAM and IgG are both members of the Ig superfamily and analogous to N-CAM, IgG binds to the NH2-terminal part of protein H. However, the binding sites for the two proteins were found to be separate, an unexpected result which was explained by the observation that the fibronectin type III (FNIII) domains and not the Ig-like domains of N-CAM are responsible for the interaction with protein H. Thus, the binding of N-CAM to protein H was blocked with fibronectin but not with IgG. Moreover, apart from fibronectin itself and N-CAM, fragments of fibronectin and the matrix protein cytotactin/tenascin containing FNIII domains also showed affinity for protein H.(ABSTRACT TRUNCATED AT 250 WORDS)

Indexed as

Bacterial ProteinsBinding SitesCarrier ProteinsCell Adhesion Molecules, NeuronalFibronectinsImmunoglobulin Fc FragmentsImmunoglobulin GMembrane ProteinsOligopeptidesProtein BindingProtein ConformationStreptococcus pyogenesStructure-Activity Relationshiparginyl-glycyl-aspartic acidBacterial ProteinsCarrier ProteinsCell Adhesion Molecules, NeuronalFibronectinsImmunoglobulin Fc FragmentsImmunoglobulin GMembrane ProteinsOligopeptidesprotein H, Streptococcus

Identifiers

PMID7737120
PMCPMC398260
OpenAlexW1836093301

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.