Evidence map›Paper›PMID 10642514›Full record

ArticleThe Biochemical journal2000

The recombinant N-terminal region of human salivary mucin MG2 (MUC7) contains a binding domain for oral Streptococci and exhibits candidacidal activity.

B Liu, S A Rayment, C Gyurko, F G Oppenheim, G D Offner, R F Troxler

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

24 citing papers in PubMed, 68 citations in OpenAlex.

  1. Trial
  2. Article
  3. Microorganisms · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. An unusual glycoform of human salivary mucin MG2.Clinical oral investigations · 2012
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. [Lacrimal gland-associated mucins. Age related production and their role in the pathophysiology of dry eye].Der Ophthalmologe : Zeitschrift der Deutschen Ophthalmologischen Gesellschaft · 2005
    Review
  19. [Tear outflow. Impact of mucins and TFF-peptides].Der Ophthalmologe : Zeitschrift der Deutschen Ophthalmologischen Gesellschaft · 2004
    Review
  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

6 authors at 2 institutions in 1 country.

B LiuDepartment of Periodontology and Oral Biology, Goldman School of Graduate Dentistry, Boston University School of Medicine, Boston University Medical Center, MA 02118, Boston, USA.
S A Rayment
C Gyurko
F G Oppenheim
G D Offner
R F Troxler
Boston University · USBoston Medical Center · US

Funding

MICROBICIDAL SALIVARY HISTIDINE-RICH PROTEINSR01DE007652 · NIDCR · BOSTON UNIVERSITY MEDICAL CAMPUS · PI OPPENHEIM, FRANK G · 1986 to 2012
$3.9M
STRUCTURE AND FUNCTION OF HUMAN SALIVARY MUCINSR01DE011691 · NIDCR · BOSTON UNIVERSITY MEDICAL CAMPUS · PI OFFNER, GWYNNETH D · 1996 to 2009
$2.8M
MUCIN AND NON-MUCIN PROTEINS IN GALLSTONE PATHOGENESISR01DK044619 · NIDDK · BOSTON UNIVERSITY MEDICAL CAMPUS · PI OFFNER, GWYNNETH D · 1992 to 2000
$212k
NIDCR NIH HHS DE07652NIDCR NIH HHS DE11691NIDDK NIH HHS DK44619
6 · The paper itself

Abstract

MG2 (the MUC7 gene product) is a low-molecular-mass mucin found in human submandibular/sublingual secretions. This mucin is believed to agglutinate a variety of microbes and thus is considered an important component of the non-immune host defence system in the oral cavity. We have shown that MUC7 can bind to cariogenic strains of Streptococcus mutans and that this binding requires a structural determinant in the N-terminal region. In the present study an expression construct, pNMuc7, encoding the N-terminal 144 amino acids of MUC7 was generated, and the recombinant protein rNMUC7 was expressed in Escherichia coli. Purified rNMUC7 was characterized and the binding of this protein to oral bacteria was investigated in an established assay. The results showed that the recombinant protein bound to S. mutans ATCC 25175 and ATCC 33402, and that alkylation of the two cysteine residues (Cys(45) and Cys(50)) resulted in the complete loss of bacterial binding. This suggests that binding of MUC7 to S. mutans occurs between the N-terminal region of the mucin molecule and the bacterial surface, and that this interaction is dependent on a cysteine-containing domain within this region of MUC7. In addition, the killing activity of rNMUC7 was compared with that of the candidacidal salivary protein histatin 5 in an established Candida albicans (ATCC 44505) blastoconidia killing assay. It was found that the LD(50) values of rNMUC7 and histatin 5 were comparable, and that the recombinant protein displayed significant killing activity at the physiological concentration range of MUC7 in whole saliva. This study is the first to show that the N-terminal region of MUC7 contains a structural determinant for bacterial binding and that this region exhibits candidacidal activity.

Indexed as

Antifungal AgentsBinding SitesCandida albicansEscherichia coliHistatinsHumansMicrobial Sensitivity TestsMouthMucinsRecombinant ProteinsReverse Transcriptase Polymerase Chain ReactionSalivary Proteins and PeptidesStreptococcus mutansAntifungal AgentsHistatinsHTN3 protein, humanMUC7 protein, humanMucinsRecombinant ProteinsSalivary Proteins and Peptides

Identifiers

PMID10642514
PMCPMC1220790
OpenAlexW2076283114

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.