Evidence map›Paper›PMID 16940404›Full record

ArticleGlycobiology2006

Characterization of a carbohydrate epitope defined by the monoclonal antibody H185: sialic acid O-acetylation on epithelial cell-surface mucins.

Pablo Argüeso, Mika Sumiyoshi

Open access · bronzeAbstract read
In one paragraph

Article in Glycobiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

28 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Ocular surface glycocalyx in health and disease.Frontiers in cell and developmental biology · 2025
    Review
  4. Article
  5. Article
  6. Human ocular mucins: The endowed guardians of sight.Advanced drug delivery reviews · 2022
    Review
  7. Review
  8. The ocular surface, coronaviruses and COVID-19.Clinical & experimental optometry · 2020
    Review
  9. Review
  10. Glycosylation pathways at the ocular surface.Biochemical Society transactions · 2018
    Review
  11. TFOS DEWS II Tear Film Report.The ocular surface · 2017
    Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Glycobiology of the ocular surface: mucins and lectins.Japanese journal of ophthalmology · 2013
    Review
  18. Article
  19. Article
  20. Review
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

2 authors at 2 institutions in 1 country.

Pablo ArgüesoSchepens Eye Research Institute and Department of Ophthalmology, Harvard Medical School, 20 Staniford Street, Boston, MA 02114-2508, USA. pablo.argueso@schepens.harvard.edu
Mika Sumiyoshi
Harvard University · USSmith-Kettlewell Eye Research Institute · US

Funding

O-Glycans on Mucins at the Ocular SurfaceR01EY014847 · NEI · SCHEPENS EYE RESEARCH INSTITUTE · PI ARGUESO, PABLO · 2003 to 2014
$4.0M
NEI NIH HHS R01 EY014847
6 · The paper itself

Abstract

Sialic acids comprise a large family of derivatives of neuraminic acid containing methyl, acetyl, sulfate, and phosphate among other groups, which confer specific physicochemical properties (e.g., hydrophobicity and resistance to hydrolases) to the molecules carrying them. Several years ago, a monoclonal antibody, designated H185, was developed, which binds to cell membranes of human corneal, conjunctival, laryngeal, and vaginal epithelia and whose distribution is altered on the ocular surface of patients with keratinizing disease. Recent findings using immunoprecipitation and immunodepletion techniques have demonstrated that, in human corneal epithelial cells, the H185 antigen is carried by the membrane-associated mucin MUC16. In this study, we show that the H185 epitope on human corneal cells and in tear fluid is an O-acetylated sialic acid epitope that can be selectively hydrolyzed in an enzyme-concentration-dependent manner by sialidase from Arthrobacter ureafaciens and to a lesser extent by sialidases from Newcastle disease virus, Clostridium perfringens, and Streptococcus pneumoniae. Binding of the H185 antibody was impaired by treatment of tear fluid with a recombinant 9-O-acetylesterase from influenza C virus. Two O-acetyl derivatives, Neu5,7Ac(2) and Neu5,9Ac(2), were identified in human tear fluid by fluorometric high-performance liquid chromatography (HPLC) and electrospray mass spectrometry (MS). Immunoprecipitation of the H185 epitope from human corneal epithelial cells revealed that Neu5,9Ac(2) was the major derivative on the mucin isolate. These results indicate that exposed wet-surfaced epithelia are decorated with O-acetyl sialic acid derivatives on membrane-associated mucins and suggest that O-acetylation on cell surfaces may protect against pathogen infection by preventing degradation of membrane-associated mucins.

Indexed as

Antibodies, MonoclonalArthrobacterBacterial ProteinsCA-125 AntigenCarbohydratesCell MembraneCells, CulturedClostridium perfringensEpithelial CellsEpithelium, CornealEpitopesHumansMembrane ProteinsN-Acetylneuraminic AcidNeuraminidaseNewcastle disease virusAntibodies, MonoclonalBacterial ProteinsCA-125 AntigenCarbohydratesEpitopesMembrane ProteinsMUC16 protein, humanN-Acetylneuraminic AcidNeuraminidaseO-acetyl sialic acidViral Proteins

Identifiers

PMID16940404
PMCPMC1976397
OpenAlexW2158435352

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.