Evidence map›Paper›PMID 18375764›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

RTX cytotoxins recognize beta2 integrin receptors through N-linked oligosaccharides.

Jana Morova, Radim Osicka, Jiri Masin, Peter Sebo

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
6.1field-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

53 citing papers in PubMed, 98 citations in OpenAlex.

  1. Covalently Linked Peptides and Membrane Potential Enable CyaA Segment Translocation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Microorganisms · 2022
    Review
  7. Article
  8. Extraintestinal PathogenicPathogens (Basel, Switzerland) · 2021
    Review
  9. Article
  10. International journal of molecular sciences · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Binding ofInternational journal of molecular sciences · 2020
    Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Review
  20. mBio · 2019
    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 3 institutions in 2 countries.

Jana MorovaInstitute of Microbiology of the Academy of Sciences of the Czech Republic, Videnska 1083, CZ-142 20 Prague 4, Czech Republic.
Radim Osicka
Jiri Masin
Peter Sebo
Harvard University · USCzech Academy of Sciences · CZCzech Academy of Sciences, Institute of Microbiology · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bordetella pertussis adenylate cyclase (AC) toxin-hemolysin (Hly) (CyaA, ACT, or AC-Hly) is a cytotoxin of the RTX (repeat in toxin) family. It delivers into target cells an AC domain that catalyzes uncontrolled conversion of ATP to cAMP, a key signaling molecule subverting phagocyte functions. CyaA utilizes a heavily N-glycosylated beta(2) integrin receptor CD11b/CD18 (alpha(M)beta(2), Mac-1, or CR3). We show that deglycosylation of cell surface proteins by glycosidase treatment, or inhibition of protein N-glycosylation by tunicamycin, ablates CyaA binding and penetration of CD11b-expressing cells. Furthermore, binding of CyaA to cells was strongly inhibited in the presence of free saccharides occurring as building units of integrin oligosaccharide complex, whereas saccharides absent from integrin oligosaccharide chains failed to inhibit CyaA binding to CD11b/CD18-expressing cells. CyaA, hence, selectively recognized sugar residues of N-linked oligosaccharides of integrins. Moreover, glycosylation of CD11a/CD18, another receptor of the beta(2) integrin family, was also essential for cytotoxic action of other RTX cytotoxins, the leukotoxin of Aggregatibacter actinomycetemcomitans (LtxA) and the Escherichia coli alpha-Hly (HlyA). These results show that binding and killing of target cells by CyaA, LtxA, and HlyA depends on recognition of N-linked oligosaccharide chains of beta(2) integrin receptors. This sets a new paradigm for action of RTX cytotoxins.

Indexed as

Adenylate Cyclase ToxinBacterial ProteinsBacterial ToxinsBinding SitesBordetellaCD11b AntigenCD18 AntigensGlycosylationHemolysin ProteinsHumansOligosaccharidesAdenylate Cyclase ToxinApxI toxin, BacteriaBacterial ProteinsBacterial ToxinsCD11b AntigenCD18 AntigensHemolysin ProteinsOligosaccharides

Identifiers

PMID18375764
PMCPMC2291121
OpenAlexW2087700316

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.