Evidence map›Paper›PMID 11705914›Full record

ArticleInfection and immunity2001

Group A streptococci bind to mucin and human pharyngeal cells through sialic acid-containing receptors.

P A Ryan, V Pancholi, V A Fischetti

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.8field-weighted citation impact, top 8% 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

35 citing papers in PubMed, 104 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Interplay between group AMicrobiology and molecular biology reviews : MMBR · 2024
    Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Surface Proteins on Gram-Positive Bacteria.Microbiology spectrum · 2019
    Review
  14. Group AMicrobiology spectrum · 2019
    Article
  15. Engineering the Mucus Barrier.Annual review of biomedical engineering · 2018
    Review
  16. Article
  17. Article
  18. Article
  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

3 authors at 2 institutions in 1 country.

P A RyanLaboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, New York 10021, USA. ryanp@mail.rockefeller.edu
V Pancholi
V A Fischetti
Rockefeller University · USPublic Health Institute · US

Funding

PROPERTIES OF STREPTOCOCCAL M PROTEINR37AI011822 · NIAID · ROCKEFELLER UNIVERSITY · PI FISCHETTI, VINCENT A. · 1987 to 2006
$2.7M
PROPERTIES OF STREPTOCOCCAL M PROTEINR01AI011822 · NIAID · ROCKEFELLER UNIVERSITY · PI FISCHETTI, VINCENT A. · 1985 to 2011
$1.7M
NIAID NIH HHS AI11822NIAID NIH HHS R01 AI011822NIAID NIH HHS R37 AI011822
6 · The paper itself

Abstract

The first step in the colonization of group A streptococci (Streptococcus pyogenes) is adherence to pharyngeal epithelial cells. Prior to adherence to their target tissue, the first barrier that the streptococci encounter is the mucous layer of the respiratory tract. The present study was undertaken to characterize the interaction between mucin, the major glycoprotein component of mucus, and streptococci. We report here that S. pyogenes is able to bind to bovine submaxillary mucin in solid-phase microtiter plate assays. Western blots probed with (125)I-labeled mucin and a panel of monoclonal antibodies revealed that the streptococcal M protein is one of two cell wall-associated proteins responsible for this binding. The binding was further localized to the N-terminal portion of the M molecule. Further analysis revealed that the M protein binds to the sialic acid moieties on mucin, and this interaction seems to be based on M-protein conformation rather than specific amino acid sequences. We found that sialic acid also plays a critical role in the adherence of an M6 streptococcal strain to the Detroit 562 human pharyngeal cell line and have identified alpha2-6-linked sialic acid as an important sialylated linkage for M-protein recognition. Western blot analysis of extracted pharyngeal cell membrane proteins identified three potential sialic acid-containing receptors for the M protein. The results are the first to show that sialic acid not only is involved in the binding of the streptococci to mucin but also plays an important role in adherence of group A streptococci to the pharyngeal cell surface.

Indexed as

Antigens, BacterialBacterial AdhesionBacterial Outer Membrane ProteinsBacterial ProteinsBinding SitesCarrier ProteinsCell LineHumansMucinsN-Acetylneuraminic AcidPharynxProtein BindingReceptors, Cell SurfaceStreptococcus pyogenesAntigens, BacterialBacterial Outer Membrane ProteinsBacterial ProteinsCarrier ProteinsMucinsN-Acetylneuraminic AcidReceptors, Cell Surfacestreptococcal M proteinstreptococcal M protein receptor

Identifiers

PMID11705914
PMCPMC98828
OpenAlexW2076549146

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.