Evidence map›Paper›PMID 1675630›Full record

ArticleInfection and immunity1991

Binding of nonspecific cross-reacting antigen, a granulocyte membrane glycoprotein, to Escherichia coli expressing type 1 fimbriae.

S L Sauter, S M Rutherfurd, C Wagener, J E Shively, S A Hefta

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

17 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
  2. Interactions of pathogenicFrontiers in immunology · 2023
    Review
  3. CEACAMs serve as toxin-stimulated receptors for enterotoxigenicProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  4. CEACAM1 in Liver Injury, Metabolic and Immune Regulation.International journal of molecular sciences · 2018
    Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. CGM1a antigen of neutrophils, a receptor of gonococcal opacity proteins.Proceedings of the National Academy of Sciences of the United States of America · 1996
    Article
  15. Article
  16. Article
  17. 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

5 authors at 2 institutions in 1 country.

S L SauterDivision of Immunology, Beckman Research Institute of the City of Hope, Duarte, California 91010.
S M Rutherfurd
C Wagener
J E Shively
S A Hefta
Beckman Research InstituteCity of Hope · US

Funding

Transgenic Mouse FacilityP30CA033572 · NCI · CITY OF HOPE/BECKMAN RESEARCH INSTITUTE · PI XIWEI WU · 1985 to 2026
$86.3M
STRUCTURE AND GENOMIC ORGANIZATION OF CEAR01CA037808 · NCI · CITY OF HOPE NATIONAL MEDICAL CENTER · PI SHIVELY, JOHN E. · 1985 to 1994
–
NCI NIH HHS CA33572NCI NIH HHS CA37808
6 · The paper itself

Abstract

Nonspecific cross-reacting antigen (NCA) is a well-characterized membrane glycoprotein on granulocytes, macrophages, and lung epithelium. Structural studies at the protein and genomic levels have revealed that NCA is a member of the immunoglobulin supergene family, and hybridization studies showed that the transcript level of NCA is induced by treatment with gamma interferon. These studies, as well as the expression of NCA on granulocytes, suggest a role for NCA in immune response. For a first step in studying this possible role, we have examined the binding of two glycoforms of NCA designated NCA-50 (Mr, 50,000) and TEX-75 (Mr, 75,000). Here we report the results from binding assays which demonstrate carbohydrate-mediated binding of Escherichia coli expressing type 1 fimbriae and of isolated type 1 fimbriae to NCA-50. TEX-75 did not bind to the purified fimbriae but bound slightly to the bacterial strain. Inhibition studies showed that the binding to NCA-50 involved interaction of mannose moieties on NCA-50 and lectins on the fimbriae. The binding of NCA-50 to bacterial fimbriae was confirmed by electron microscopy studies, using immunolabeling techniques. In addition, we show that the surface expression of NCA-50 (and presumably of other NCA species) on isolated polymorphonuclear leukocytes is increased following activation with the bacterial peptide formylmethionyl-leucyl-phenylalanine, consistent with a role for NCA in immune response.

Indexed as

Antigens, NeoplasmCell Adhesion MoleculesBacterial AdhesionCarbohydratesEscherichia coliFimbriae, BacterialHumansIn Vitro TechniquesMembrane GlycoproteinsMicroscopy, ElectronN-Formylmethionine Leucyl-PhenylalanineProtein BindingAntigens, NeoplasmCarbohydratesCell Adhesion MoleculesMembrane GlycoproteinsN-Formylmethionine Leucyl-Phenylalanine

Identifiers

PMID1675630
PMCPMC258036
OpenAlexW2109846475

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.